Molecular properties and modifications of some respiratory and nutritional allergens

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Molecular properties and modifications of some respiratory and nutritional allergens (en)
Молекуларне особине и модификације неких респираторних и нутритивних алергена (sr)
Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (sr_RS)
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Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu

Prodić, Ivana

(Универзитет у Београду, Хемијски факултет, 2019)

TY  - THES
AU  - Prodić, Ivana
PY  - 2019
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=7705
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:22917/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=23935753
UR  - https://nardus.mpn.gov.rs/handle/123456789/17617
UR  - http://intor.torlakinstitut.com/handle/123456789/777
AB  - INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije.
AB  - INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu
UR  - https://hdl.handle.net/21.15107/rcub_intor_777
ER  - 
@phdthesis{
author = "Prodić, Ivana",
year = "2019",
abstract = "INFOGEST metoda predstavlja standardizovani protokol za in vitro simulacijudigestije kompletne hrane, zasnovanom na fiziološki relevantnim uslovima. Predmetrada ove disertacije je ispitivanje digestibilnosti alergena kikirikija iz celog zrnaprimenom INFOGEST metode, kao i karakterizacija njihovih fragmenata otpornih naproteolizu.Za odstranjivanje lipida primenjena je metoda taloženja proteina, koja se pokazala kaosuperiornija u odnosu ekstrakciju lipida organskim rastvaračem, usled manjegkvalitativnog i kvantitativnog gubitka proteina.U ovoj tezi je pokazano da termički tretmani kikirikija, pored matriksa hrane, dodatnootežavaju oslobađanje proteina iz zrna, što čini glavne alergene kikirikija Ara h 1, Ara h2 Ara h 3 i Ara h 6 nedostupnijim za pepsinsku hidrolizu. Oslobađanje proteinakikirikija, kao i digestibilnost, u gastričnoj fazi se pokazala znatno izraženijom, uodnosu na intestinalnu fazu, s tim da je digestija kod pečenog kikirikija otežana uodnosu na sirovi. Nakon oralno-gastrične digestije celog zrna sirovog kikirikija, glavnialergeni kikirikija u velikoj meri ostaju intaktni, a njihovi peptidi otporni na digestijuzadržavaju alergeni kapacitet. Pokazano je da većina Ara h 2 i Ara h 6 alergena ostajerezistentna na digestiju. Ara h 1 i Ara h 3 kaskadno podležu pepsinolizi, do fragmenatakoji i dalje zadržavaju IgE vezujući potencijal. Mali peptidi koji potiču od Ara h 2alergena, su se pokazali kao najpotentniji inhibitori vezivanja IgE iz seruma pacijenataalergičnih na kikiriki, u odnosu na male Ara h 1 i Ara h 3 peptide.U ovoj disertaciji je pokazana izuzetno važna uloga efekata matriksa hrane, kao i njenetermičke obrade, na digestiju proteina hrane, koji mogu povećati stabilnost alergenahrane tokom digestije, i time omogućiti zadržavanje potencijala aktivacije alergijskereakcije nakon oralno-gastrične faze digestije., INFOGEST method is standardized protocol for in vitro simulation of complete fooddigestion, based on physiologicaly relevant conditions. The objective of thisdissertation was to investigate digestibility of peanut allergens from whole peanutkernel by INFOGEST method, as well as to characterize their fragments resistant toproteolysis.For delipidation, protein precipitation approach was applied, showing to be superior incomparison to delipidation by organic solevent, due to lower qualitative andquantitative protein loss.In this thesis it was shown that peanut thermal processing, in addition to effect of foodmatix, further complicates the extractability and digestibility of proteins from the grain,making peanut allergens Ara h 1, 2, 3 and 6, less accessible for pepsin hydrolysis.Extractability and digestibility of peanut proteins in the gastric phase have shown to besignificantly more pronounced, in comparison to intestinal phase, and roasted peanutdigestion was impaired compared to the raw. It was shown that after oral and gastricdigestion of whole raw peanut grains peanut allergens largely remain intact, and theirdigestion resistant peptides retain allergenic capacity. The most Ara h 2 and Ara h 6allergens have been shown to remain resistant to digestion. Ara h 1 and Ara h 3undergo pepsinolysis with cascade pattern to consequently smaller peptide fragmentswith retained IgE binding capacity. Small peptides from Ara h 2 allergens were themost potent inhibitors of IgE binding from sera of peanut allergic patients, compared tosmall peptides from Ara h 1 and Ara h 3.This thesis points to the great importance of the effects of food matrix, as well as foodthermal processing, on protein digestibility, which can create additional stability offood allergens during digestion, and thus enable retaining of their potential for thesensitization or triggering of allergic reactions.",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu",
url = "https://hdl.handle.net/21.15107/rcub_intor_777"
}
Prodić, I.. (2019). Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_intor_777
Prodić I. Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu. in Универзитет у Београду. 2019;.
https://hdl.handle.net/21.15107/rcub_intor_777 .
Prodić, Ivana, "Digestomika alergena kikirikija i karakterizacija fragmenata otpornih na proteolizu" in Универзитет у Београду (2019),
https://hdl.handle.net/21.15107/rcub_intor_777 .

Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment

Peruško, Marija; Simović, Ana; Stevanović, Nikola; Smiljanić, Katarina; Radomirović, Mirjana Ž.; Stanić-Vučinić, Dragana; Ghnimi, Sami; Ćirković-Veličković, Tanja

(The Faculty of Sciences, University of Novi Sad, Serbian proteomic association, 2019)

TY  - CONF
AU  - Peruško, Marija
AU  - Simović, Ana
AU  - Stevanović, Nikola
AU  - Smiljanić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Stanić-Vučinić, Dragana
AU  - Ghnimi, Sami
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/783
AB  - Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demandfor camel milk has increased worldwide.Production of camel milk powders facilitate its transport,prolonge shelf-life, and also offer an attractive additive for various food products. In this study wecharacterized proteins of soluble fraction of freeze/spray dried camel milk powders.Material and Methods: Whole camel milk powders were prepared by spray drying treatment at sixdifferent inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions uponthe treatments were analysed by combination of electrophoretic techniques and circular dichroism.Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while nativeelectrophoresis revealed non-uniform decrease in pI values with increased inlet temperature ofspray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectrashowed no differences in secondary structures between freeze and spray dried samples. Massspectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serumalbumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and onimmunoglobulin heavy chain.Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spraydrying treatment which further may affect techno-functional properties of camel milk powders,their shelf-life and nutritional value.Acknowledgments: This work was supported by the Ministry of Education, Science andTechnological Development of the Republic of Serbia, grant number 172024. The project leading tothis application has received funding from the European Union's Horizon 2020 research andinnovation programme under grant agreement No 810752.
PB  - The Faculty of Sciences, University of Novi Sad, Serbian proteomic association
C3  - The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
T1  - Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment
EP  - 7
SP  - 7
UR  - https://hdl.handle.net/21.15107/rcub_intor_783
ER  - 
@conference{
author = "Peruško, Marija and Simović, Ana and Stevanović, Nikola and Smiljanić, Katarina and Radomirović, Mirjana Ž. and Stanić-Vučinić, Dragana and Ghnimi, Sami and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demandfor camel milk has increased worldwide.Production of camel milk powders facilitate its transport,prolonge shelf-life, and also offer an attractive additive for various food products. In this study wecharacterized proteins of soluble fraction of freeze/spray dried camel milk powders.Material and Methods: Whole camel milk powders were prepared by spray drying treatment at sixdifferent inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions uponthe treatments were analysed by combination of electrophoretic techniques and circular dichroism.Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry.Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while nativeelectrophoresis revealed non-uniform decrease in pI values with increased inlet temperature ofspray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectrashowed no differences in secondary structures between freeze and spray dried samples. Massspectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1(GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serumalbumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne(CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and onimmunoglobulin heavy chain.Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spraydrying treatment which further may affect techno-functional properties of camel milk powders,their shelf-life and nutritional value.Acknowledgments: This work was supported by the Ministry of Education, Science andTechnological Development of the Republic of Serbia, grant number 172024. The project leading tothis application has received funding from the European Union's Horizon 2020 research andinnovation programme under grant agreement No 810752.",
publisher = "The Faculty of Sciences, University of Novi Sad, Serbian proteomic association",
journal = "The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia",
title = "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment",
pages = "7-7",
url = "https://hdl.handle.net/21.15107/rcub_intor_783"
}
Peruško, M., Simović, A., Stevanović, N., Smiljanić, K., Radomirović, M. Ž., Stanić-Vučinić, D., Ghnimi, S.,& Ćirković-Veličković, T.. (2019). Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia
The Faculty of Sciences, University of Novi Sad, Serbian proteomic association., 7-7.
https://hdl.handle.net/21.15107/rcub_intor_783
Peruško M, Simović A, Stevanović N, Smiljanić K, Radomirović MŽ, Stanić-Vučinić D, Ghnimi S, Ćirković-Veličković T. Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment. in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia. 2019;:7-7.
https://hdl.handle.net/21.15107/rcub_intor_783 .
Peruško, Marija, Simović, Ana, Stevanović, Nikola, Smiljanić, Katarina, Radomirović, Mirjana Ž., Stanić-Vučinić, Dragana, Ghnimi, Sami, Ćirković-Veličković, Tanja, "Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment" in The book of abstracts, V SePA symposium: Proteomics in the analysis of food, environmental protection and medical research, 31.5.2019, Novi Sad, Serbia (2019):7-7,
https://hdl.handle.net/21.15107/rcub_intor_783 .

Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products

Prodić, Ivana; Smiljanić, Katarina; Mihailović, Jelena; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(Univerzitet u Beogradu - Hemijski fakultet, 2019)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/775
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
EP  - 25
SP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_intor_775
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_intor_775"
}
Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_intor_775
Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_intor_775 .
Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_intor_775 .

Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)

Mihailović, Jelena; Prodić, Ivana; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Serbian Proteomic Association - SePA, 2019)

TY  - CONF
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/770
AB  - Introduction. Peanut allergy affects a large portion of world population causing reactions rangingfrom mild to severe. Major peanut allergen IgE epitopes are well characterized but little is knownabout their post-translational modifications (PTM) and how they are affected by thermaltreatment. PTM profile may differ between raw and thermally treated peanut, which could affectits allergic potential depending on type, size and position of modifications.Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-upproteomics methods.Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digestedin gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (ThermoFisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 andAra h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the ImmuneEpitope Database (IEDB www.iedb.org).Main findings. LFQ results show that there is no significant change in the amountsof any of thestudied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in thehighest portion, with respect to the protein size: 15% and 12% of its positions are modified in rawand roasted sample, respectively. Total of 21 modifications were quantified between the twopreparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largestnumber of peptides.Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern andquantity between treated and non-treated extracts. The in silico discovered PTMs could affectprotein digestibility and allergenicity. Further investigation is necessary in order to fully understandthe impact protein modifications could have on their allergenic potential.
PB  - Serbian Proteomic Association - SePA
C3  - Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
T1  - Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)
SP  - 16/L10
UR  - https://hdl.handle.net/21.15107/rcub_intor_770
ER  - 
@conference{
author = "Mihailović, Jelena and Prodić, Ivana and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Introduction. Peanut allergy affects a large portion of world population causing reactions rangingfrom mild to severe. Major peanut allergen IgE epitopes are well characterized but little is knownabout their post-translational modifications (PTM) and how they are affected by thermaltreatment. PTM profile may differ between raw and thermally treated peanut, which could affectits allergic potential depending on type, size and position of modifications.Objective. Our aim was to analyse and compare PTM profiles of 4 major peanut allergens - Ara h 1,Ara h 2, Ara h 3 and Ara h 6, as well as their amounts in raw and roasted samples using bottom-upproteomics methods.Methodology. Full peanut protein extracts (both thermally treated and non-treated) were digestedin gel and in solution, and analysed by a Top10 nLC-MS/MS method by LTQ Orbitrap XL (ThermoFisher Scientific Inc., Germany). Within the extracts major allergens - Ara h 1, Ara h 2, Ara h 3 andAra h 6 were identified, label free quantified (LFQ) and searched for PTMs by Peaks X software(Bioinformatics solutions Inc.I, Canada). Epitope sequences were acquired from the ImmuneEpitope Database (IEDB www.iedb.org).Main findings. LFQ results show that there is no significant change in the amountsof any of thestudied allergens between raw and roasted extracts.Out of the 4 allergens Ara h 6 is modified in thehighest portion, with respect to the protein size: 15% and 12% of its positions are modified in rawand roasted sample, respectively. Total of 21 modifications were quantified between the twopreparations, with oxidation (M), methylation (K,R) and dethiomethylation affecting the largestnumber of peptides.Conclusions. Peanut allergen epitopes are indeed carriers of PTMs that differ in pattern andquantity between treated and non-treated extracts. The in silico discovered PTMs could affectprotein digestibility and allergenicity. Further investigation is necessary in order to fully understandthe impact protein modifications could have on their allergenic potential.",
publisher = "Serbian Proteomic Association - SePA",
journal = "Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019",
title = "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)",
pages = "16/L10",
url = "https://hdl.handle.net/21.15107/rcub_intor_770"
}
Mihailović, J., Prodić, I., Smiljanić, K.,& Ćirković-Veličković, T.. (2019). Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019
Serbian Proteomic Association - SePA., 16/L10.
https://hdl.handle.net/21.15107/rcub_intor_770
Mihailović J, Prodić I, Smiljanić K, Ćirković-Veličković T. Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs). in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019. 2019;:16/L10.
https://hdl.handle.net/21.15107/rcub_intor_770 .
Mihailović, Jelena, Prodić, Ivana, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Comparative study of raw and thermally treated peanut major allergen post- translational modifications (PTMs)" in Book of Abstracts - V SePa Simposium: Proteomics in the analysis of food, environmental protection and medical research, Novi Sad 2019 (2019):16/L10,
https://hdl.handle.net/21.15107/rcub_intor_770 .

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/536
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
EP  - 658
SP  - 644
VL  - 126
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
pages = "658-644",
volume = "126",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Pergamon-Elsevier Science Ltd, Oxford., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer L, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija, Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .
2
15
5
15

Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Radosavljević, Jelena; Mihailović, Jelena; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Srpsko Udruženje za Proteomiku; IBISS, 2018)

TY  - CONF
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Radosavljević, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/789
AB  - Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsindigestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published astandardized static digestion method for food, based on physiological conditions emphasizing theimpact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestionresistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract isexposed during digestion of peanut proteins, has not been investigated under pure physiologicalconditions suggested by this protocol.Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, wereused to identify and characterize peanut digesta.Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitopesequences found via Immune Epitope Database (www.iedb.org).Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occursimultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, largeand short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly
PB  - Srpsko Udruženje za Proteomiku; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix
UR  - https://hdl.handle.net/21.15107/rcub_intor_789
ER  - 
@conference{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Radosavljević, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Major peanut allergens, Ara h 2 and Ara h 6, are known to be resistant to pepsindigestion, and they sensitize individual via the gastrointestinal tract. Mikenus et al. published astandardized static digestion method for food, based on physiological conditions emphasizing theimpact of food matrices. Immunoreactive proteins (large fragments) and peptides (short digestionresistant peptides SDRPs; <10 kDa), to which the immune system of the gastrointestinal tract isexposed during digestion of peanut proteins, has not been investigated under pure physiologicalconditions suggested by this protocol.Matherial and methods: Whole grain of grounded raw peanut was incubated with human α-amylase, and pepsin, mimicking the effects of oral and gastric digestion, in total duration of 2h.Bottom up proteomic approach, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, wereused to identify and characterize peanut digesta.Results: After 2h of oral/gastric phase we got, intact proteins, large, digestion resistant peptides(DRP) and SDRPs, as well. Ara h 2 and Ara h 6 remained mostly intact, and short DRPs from Ara h2 and Ara h 6 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h3 showed preserved allergenic capacity, as well. Almost all of identified short DRPs from Ara h 1,Ara h 2 and Ara h 3, with preserved allergenic potential, were constituents of continuous epitopesequences found via Immune Epitope Database (www.iedb.org).Conclusion: Processes of protein extraction from the matrix and their enzymatic digestion occursimultaneously. Oral and gastric phase digestion products of raw peanut are intact proteins, largeand short digestion resistant peptides. Under these conditions Ara h 2 and Ara h 6 are expectedly",
publisher = "Srpsko Udruženje za Proteomiku; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix",
url = "https://hdl.handle.net/21.15107/rcub_intor_789"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Radosavljević, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku; IBISS..
https://hdl.handle.net/21.15107/rcub_intor_789
Prodić I, Stanić-Vučinić D, Apostolović D, Radosavljević J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;.
https://hdl.handle.net/21.15107/rcub_intor_789 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Radosavljević, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Gastric digestome of whole peanut grains from the aspect of immunoproteomics: Characterization of digested allergens in the real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018),
https://hdl.handle.net/21.15107/rcub_intor_789 .

Digestomics of Japanese abalone in real food matrix

Prodić, Ivana; Khulal, Urmila; Mutić, Jelena; Mihailović, Jelena; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Srpsko Udruženje za Proteomiku, SePA; IBISS, 2018)

TY  - CONF
AU  - Prodić, Ivana
AU  - Khulal, Urmila
AU  - Mutić, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/774
AB  - Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Digestomics of Japanese abalone in real food matrix
EP  - 10
SP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_intor_774
ER  - 
@conference{
author = "Prodić, Ivana and Khulal, Urmila and Mutić, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Digestomics of Japanese abalone in real food matrix",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_intor_774"
}
Prodić, I., Khulal, U., Mutić, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 10-10.
https://hdl.handle.net/21.15107/rcub_intor_774
Prodić I, Khulal U, Mutić J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:10-10.
https://hdl.handle.net/21.15107/rcub_intor_774 .
Prodić, Ivana, Khulal, Urmila, Mutić, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Digestomics of Japanese abalone in real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):10-10,
https://hdl.handle.net/21.15107/rcub_intor_774 .

Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination

Smiljanić, Katarina; Prodić, Ivana; Aleksić, Ivana; Veljović, Đorđe; Ćirković-Veličković, Tanja; Mutić, Jelena; Burazer, Lidija M.

(Srpsko Udruženje za Proteomiku, SePA; IBISS, 2018)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Aleksić, Ivana
AU  - Veljović, Đorđe
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Burazer, Lidija M.
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/772
AB  - Objective: to create method for unrestrictive deep, relative quantification of post translationalmodifications (PTMs) within different proteomes. Pollution field studies of bio indicators such aspollen are valuable because of realistic situation of target contamination, however they carry thegreat extent of uncertainty in attributing and delineating the polluting effect from multiple sources.Holistic research platform focusing on comprehensively characterized and quantified PTMs ofcomparable bio-indicator proteomes could help and overcome these obstacles of field pollutionstudies.Material and Methods: Scanning electron and light microscopy assessed surface and sub pollenparticle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emissionspectrometry revealed metal elemental content in pollen while in solution trypsin digested pollenproteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5brought quantitative information on protein expression level and its PTM profiling.Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPPreleasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hgand Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),including actin, were upregulated several times in polluted sample compared to ecologicallypreserved pollen (P1). While the level of spontaneous and physiological PTMs includingmethylation, acetylation, deamidation and formylation, was similar without significant changes inP1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexoseadducts showed several times higher and significant increase in abundancy of P2 compared to P1.PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.Conclusion: Results suggest prominent role of chemical pollution compared to effect of road trafficpollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium(Cd).
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination
EP  - 13
SP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_intor_772
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Aleksić, Ivana and Veljović, Đorđe and Ćirković-Veličković, Tanja and Mutić, Jelena and Burazer, Lidija M.",
year = "2018",
abstract = "Objective: to create method for unrestrictive deep, relative quantification of post translationalmodifications (PTMs) within different proteomes. Pollution field studies of bio indicators such aspollen are valuable because of realistic situation of target contamination, however they carry thegreat extent of uncertainty in attributing and delineating the polluting effect from multiple sources.Holistic research platform focusing on comprehensively characterized and quantified PTMs ofcomparable bio-indicator proteomes could help and overcome these obstacles of field pollutionstudies.Material and Methods: Scanning electron and light microscopy assessed surface and sub pollenparticle (SPP) releasing features of timothy grass (TG) pollen. Inductively coupled atomic emissionspectrometry revealed metal elemental content in pollen while in solution trypsin digested pollenproteomes analysed with high resolution Orbitrap mass tandem spectrometry and PEAKS Suite 8.5brought quantitative information on protein expression level and its PTM profiling.Results: TG polluted pollen samples (P2) collected along regional road and chemical plant,exposed to air contaminants from road traffics and chemical plants showed 4.5 times higher SPPreleasing capacity, with notable surface changes, as well as significantly higher contents of Mn, Hgand Cd. Antioxidative enzymes (oxidoreductases, superoxide dismutases and peroxidases),including actin, were upregulated several times in polluted sample compared to ecologicallypreserved pollen (P1). While the level of spontaneous and physiological PTMs includingmethylation, acetylation, deamidation and formylation, was similar without significant changes inP1 and P2 pollens, oxidative PTMs including oxidation of Met, Lys, His, Pro and HNE and hexoseadducts showed several times higher and significant increase in abundancy of P2 compared to P1.PTMs connected to road traffic such as tyrosine nitration were very rare and low abundant.Conclusion: Results suggest prominent role of chemical pollution compared to effect of road trafficpollution, with primary consequences from oxidative properties of mercury (Hg) and cadmium(Cd).",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_intor_772"
}
Smiljanić, K., Prodić, I., Aleksić, I., Veljović, Đ., Ćirković-Veličković, T., Mutić, J.,& Burazer, L. M.. (2018). Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 13-13.
https://hdl.handle.net/21.15107/rcub_intor_772
Smiljanić K, Prodić I, Aleksić I, Veljović Đ, Ćirković-Veličković T, Mutić J, Burazer LM. Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:13-13.
https://hdl.handle.net/21.15107/rcub_intor_772 .
Smiljanić, Katarina, Prodić, Ivana, Aleksić, Ivana, Veljović, Đorđe, Ćirković-Veličković, Tanja, Mutić, Jelena, Burazer, Lidija M., "Deep and quantitative profiling of PTMs in ecologically preserved and polluted pollen proteomes of timothy grass reveals predominant source of contamination" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):13-13,
https://hdl.handle.net/21.15107/rcub_intor_772 .

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/608
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .
3
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41

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/514
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .
3
40
24
41

Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up

Živanović, Mirjana; Atanasković-Marković, Marina; Međo, Biljana; Gavrović-Jankulović, Marija; Smiljanić, Katarina; Tmušić, Vladimir; Đurić, Vojislav

(Iranian Scientific Society Medical Entomology, Tehran, 2017)

TY  - JOUR
AU  - Živanović, Mirjana
AU  - Atanasković-Marković, Marina
AU  - Međo, Biljana
AU  - Gavrović-Jankulović, Marija
AU  - Smiljanić, Katarina
AU  - Tmušić, Vladimir
AU  - Đurić, Vojislav
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/785
AB  - IgE-mediated food allergy affects 6-8% of children. Our study aimed to define the correlations between the results obtained with skin prick tests (SPTs) using commercial extracts and fresh foods, and the correlations between these result and those obtained with specific IgE (sIgE) and/or challenge. Children aged from 2 months to 6 years were recruited prospectively. Overall 571 children were positive to one food. In all children we performed SPT using commercial extracts of suspected food and fresh foods and sIgE. If SPT and sIgE test results did not correspond to the history, we performed open oral food challenge. Sensitivity of SPT with commercial extracts for all tested food was poor (3-35%), while sensitivity of fresh food skin prick tests (FFSPT) was excellent (50-100%), and showed correlation with open oral food challenge (p lt 0.001). Our results suggest that fresh food extracts are more effective in detecting sensitization and with levels of sIgE greater than class 3 could predict clinical reactivity, without the need for potentially hazardous food challenges.
PB  - Iranian Scientific Society Medical Entomology, Tehran
T2  - Iranian Journal of Allergy Asthma and Immunology
T1  - Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up
EP  - 132
IS  - 2
SP  - 127
VL  - 16
UR  - https://hdl.handle.net/21.15107/rcub_intor_785
ER  - 
@article{
author = "Živanović, Mirjana and Atanasković-Marković, Marina and Međo, Biljana and Gavrović-Jankulović, Marija and Smiljanić, Katarina and Tmušić, Vladimir and Đurić, Vojislav",
year = "2017",
abstract = "IgE-mediated food allergy affects 6-8% of children. Our study aimed to define the correlations between the results obtained with skin prick tests (SPTs) using commercial extracts and fresh foods, and the correlations between these result and those obtained with specific IgE (sIgE) and/or challenge. Children aged from 2 months to 6 years were recruited prospectively. Overall 571 children were positive to one food. In all children we performed SPT using commercial extracts of suspected food and fresh foods and sIgE. If SPT and sIgE test results did not correspond to the history, we performed open oral food challenge. Sensitivity of SPT with commercial extracts for all tested food was poor (3-35%), while sensitivity of fresh food skin prick tests (FFSPT) was excellent (50-100%), and showed correlation with open oral food challenge (p lt 0.001). Our results suggest that fresh food extracts are more effective in detecting sensitization and with levels of sIgE greater than class 3 could predict clinical reactivity, without the need for potentially hazardous food challenges.",
publisher = "Iranian Scientific Society Medical Entomology, Tehran",
journal = "Iranian Journal of Allergy Asthma and Immunology",
title = "Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up",
pages = "132-127",
number = "2",
volume = "16",
url = "https://hdl.handle.net/21.15107/rcub_intor_785"
}
Živanović, M., Atanasković-Marković, M., Međo, B., Gavrović-Jankulović, M., Smiljanić, K., Tmušić, V.,& Đurić, V.. (2017). Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up. in Iranian Journal of Allergy Asthma and Immunology
Iranian Scientific Society Medical Entomology, Tehran., 16(2), 127-132.
https://hdl.handle.net/21.15107/rcub_intor_785
Živanović M, Atanasković-Marković M, Međo B, Gavrović-Jankulović M, Smiljanić K, Tmušić V, Đurić V. Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up. in Iranian Journal of Allergy Asthma and Immunology. 2017;16(2):127-132.
https://hdl.handle.net/21.15107/rcub_intor_785 .
Živanović, Mirjana, Atanasković-Marković, Marina, Međo, Biljana, Gavrović-Jankulović, Marija, Smiljanić, Katarina, Tmušić, Vladimir, Đurić, Vojislav, "Evaluation of Food Allergy in Children by Skin Prick Tests with Commercial Extracts and Fresh Foods, Specific IgE and, Open Oral Food Challenge: Our Five Years Experience in Food Allergy Work-up" in Iranian Journal of Allergy Asthma and Immunology, 16, no. 2 (2017):127-132,
https://hdl.handle.net/21.15107/rcub_intor_785 .
7
11

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Perusko, Marija; Al-Hanish, Ayah; Mihailović, Jelena; Minić, Simeon; Trifunović, Sara; Prodić, Ivana; Cirkovic Velicković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - JOUR
AU  - Perusko, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović, Jelena
AU  - Minić, Simeon
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Cirkovic Velicković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/757
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
EP  - 752
SP  - 744
VL  - 232
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 
@article{
author = "Perusko, Marija and Al-Hanish, Ayah and Mihailović, Jelena and Minić, Simeon and Trifunović, Sara and Prodić, Ivana and Cirkovic Velicković, Tanja",
year = "2017",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
pages = "752-744",
volume = "232",
doi = "10.1016/j.foodchem.2017.04.074"
}
Perusko, M., Al-Hanish, A., Mihailović, J., Minić, S., Trifunović, S., Prodić, I.,& Cirkovic Velicković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074
Perusko M, Al-Hanish A, Mihailović J, Minić S, Trifunović S, Prodić I, Cirkovic Velicković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752.
doi:10.1016/j.foodchem.2017.04.074 .
Perusko, Marija, Al-Hanish, Ayah, Mihailović, Jelena, Minić, Simeon, Trifunović, Sara, Prodić, Ivana, Cirkovic Velicković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 . .
34
24
34

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, S.; Ognjenović, Jana; Perusko, M.; Mihajlović, Luka; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, S.
AU  - Ognjenović, Jana
AU  - Perusko, M.
AU  - Mihajlović, Luka
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/610
AB  - Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
EP  - 828
IS  - 6
SP  - 815
VL  - 47
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, S. and Ognjenović, Jana and Perusko, M. and Mihajlović, Luka and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
pages = "828-815",
number = "6",
volume = "47",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S., Ognjenović, J., Perusko, M., Mihajlović, L., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović S, Ognjenović J, Perusko M, Mihajlović L, Burazer L, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, S., Ognjenović, Jana, Perusko, M., Mihajlović, Luka, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .
2
24
15
21

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, S.; Ognjenović, Jana; Perusko, M.; Mihajlović, Luka; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, S.
AU  - Ognjenović, Jana
AU  - Perusko, M.
AU  - Mihajlović, Luka
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/479
AB  - Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
EP  - 828
IS  - 6
SP  - 815
VL  - 47
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, S. and Ognjenović, Jana and Perusko, M. and Mihajlović, Luka and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
pages = "828-815",
number = "6",
volume = "47",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S., Ognjenović, J., Perusko, M., Mihajlović, L., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović S, Ognjenović J, Perusko M, Mihajlović L, Burazer L, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, S., Ognjenović, Jana, Perusko, M., Mihajlović, Luka, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .
2
24
15
21

Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/759
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
EP  - 250
SP  - 241
VL  - 61
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
pages = "250-241",
volume = "61",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T.. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids. 2016;61:241-250.
doi:10.1016/j.foodhyd.2016.05.012 .
Al-Hanish, Ayah, Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Prodić, Ivana, Minić, Simeon L., Stojadinović, Marija M., Radibratović, Milica, Milčić, Miloš K., Ćirković-Veličković, Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" in Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 . .
2
105
63
110

Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation

Stanić-Vučinić, Dragana; Stojadinović, Marija; Mirkov, Ivana; Apostolović, Danijela; Burazer, Lidija; Atanasković-Marković, Marina; Kataranovski, Milena; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/456
AB  - Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation
EP  - 88228
IS  - 91
SP  - 88216
VL  - 6
DO  - 10.1039/c6ra17261j
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation",
pages = "88228-88216",
number = "91",
volume = "6",
doi = "10.1039/c6ra17261j"
}
Stanić-Vučinić, D., Stojadinović, M., Mirkov, I., Apostolović, D., Burazer, L., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(91), 88216-88228.
https://doi.org/10.1039/c6ra17261j
Stanić-Vučinić D, Stojadinović M, Mirkov I, Apostolović D, Burazer L, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances. 2016;6(91):88216-88228.
doi:10.1039/c6ra17261j .
Stanić-Vučinić, Dragana, Stojadinović, Marija, Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija, Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation" in RSC Advances, 6, no. 91 (2016):88216-88228,
https://doi.org/10.1039/c6ra17261j . .
1
1
1

Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles

Mihajlović, Luka; Radosavljević, Jelena; Burazer, Lidija; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2015)

TY  - JOUR
AU  - Mihajlović, Luka
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://intor.torlakinstitut.com/handle/123456789/451
AB  - Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles
EP  - 132
SP  - 125
VL  - 109
DO  - 10.1016/j.phytochem.2014.10.022
ER  - 
@article{
author = "Mihajlović, Luka and Radosavljević, Jelena and Burazer, Lidija and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2015",
abstract = "Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles",
pages = "132-125",
volume = "109",
doi = "10.1016/j.phytochem.2014.10.022"
}
Mihajlović, L., Radosavljević, J., Burazer, L., Smiljanić, K.,& Ćirković-Veličković, T.. (2015). Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 109, 125-132.
https://doi.org/10.1016/j.phytochem.2014.10.022
Mihajlović L, Radosavljević J, Burazer L, Smiljanić K, Ćirković-Veličković T. Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry. 2015;109:125-132.
doi:10.1016/j.phytochem.2014.10.022 .
Mihajlović, Luka, Radosavljević, Jelena, Burazer, Lidija, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles" in Phytochemistry, 109 (2015):125-132,
https://doi.org/10.1016/j.phytochem.2014.10.022 . .
34
20
33

The importance of cross-reactivity in grass pollen allergy

Aleksić, Ivana; Vučković, Olga; Smiljanić, Katarina; Gavrović-Jankulović, Marija; Krsmanović, Vera; Burazer, Lidija

(Srpsko biološko društvo, Beograd, i dr., 2014)

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Vučković, Olga
AU  - Smiljanić, Katarina
AU  - Gavrović-Jankulović, Marija
AU  - Krsmanović, Vera
AU  - Burazer, Lidija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/407
AB  - According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - The importance of cross-reactivity in grass pollen allergy
EP  - 1155
IS  - 3
SP  - 1149
VL  - 66
DO  - 10.2298/ABS1403149A
ER  - 
@article{
author = "Aleksić, Ivana and Vučković, Olga and Smiljanić, Katarina and Gavrović-Jankulović, Marija and Krsmanović, Vera and Burazer, Lidija",
year = "2014",
abstract = "According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "The importance of cross-reactivity in grass pollen allergy",
pages = "1155-1149",
number = "3",
volume = "66",
doi = "10.2298/ABS1403149A"
}
Aleksić, I., Vučković, O., Smiljanić, K., Gavrović-Jankulović, M., Krsmanović, V.,& Burazer, L.. (2014). The importance of cross-reactivity in grass pollen allergy. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(3), 1149-1155.
https://doi.org/10.2298/ABS1403149A
Aleksić I, Vučković O, Smiljanić K, Gavrović-Jankulović M, Krsmanović V, Burazer L. The importance of cross-reactivity in grass pollen allergy. in Archives of Biological Sciences. 2014;66(3):1149-1155.
doi:10.2298/ABS1403149A .
Aleksić, Ivana, Vučković, Olga, Smiljanić, Katarina, Gavrović-Jankulović, Marija, Krsmanović, Vera, Burazer, Lidija, "The importance of cross-reactivity in grass pollen allergy" in Archives of Biological Sciences, 66, no. 3 (2014):1149-1155,
https://doi.org/10.2298/ABS1403149A . .
3
1
3

Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions

Stanić-Vučinić, Dragana; Prodić, Ivana; Apostolović, Danijela; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/761
AB  - Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions
EP  - 599
IS  - 1
SP  - 590
VL  - 138
DO  - 10.1016/j.foodchem.2012.10.087
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Prodić, Ivana and Apostolović, Danijela and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions",
pages = "599-590",
number = "1",
volume = "138",
doi = "10.1016/j.foodchem.2012.10.087"
}
Stanić-Vučinić, D., Prodić, I., Apostolović, D., Nikolić, M.,& Ćirković-Veličković, T.. (2013). Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 138(1), 590-599.
https://doi.org/10.1016/j.foodchem.2012.10.087
Stanić-Vučinić D, Prodić I, Apostolović D, Nikolić M, Ćirković-Veličković T. Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. in Food Chemistry. 2013;138(1):590-599.
doi:10.1016/j.foodchem.2012.10.087 .
Stanić-Vučinić, Dragana, Prodić, Ivana, Apostolović, Danijela, Nikolić, Milan, Ćirković-Veličković, Tanja, "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions" in Food Chemistry, 138, no. 1 (2013):590-599,
https://doi.org/10.1016/j.foodchem.2012.10.087 . .
103
79
113

Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions

Stanić-Vučinić, Dragana; Prodić, Ivana; Apostolović, Danijela; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/762
AB  - Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions
EP  - 599
IS  - 1
SP  - 590
VL  - 138
DO  - 10.1016/j.foodchem.2012.10.087
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Prodić, Ivana and Apostolović, Danijela and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Sonication is a new processing technology in the dairy industry. The aim of this study was to test glycation of beta-lactoglobulin (BLG) in Maillard reaction (MR) induced by high-intensity ultrasound in aqueous solution under neutral conditions at 10-15 degrees C, which is not favourable for the MR. BLG was sonicated in the presence of glucose, galactose, lactose, fructose, ribose and arabinose. Formation of Maillard reaction products (MRPs) was monitored by mass spectrometry, spectrophotometry and fluorimetry. Ultrasound treatment resulted in formation of MRPs with all tested carbohydrates. Ribose induced the highest degree of modification resulting in 76% of BLG modified and an average of three anhydroribose units attached. Circular dichroism spectra analyses indicated only minor alterations in secondary and tertiary structures. MRP obtained by ultrasound exhibited 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity and possessed increased iron-chelating activity and reducing power. High-intensity ultrasound efficiently promotes BLG-glycoconjugates formation by MR in aqueous solutions under non-denaturing conditions.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions",
pages = "599-590",
number = "1",
volume = "138",
doi = "10.1016/j.foodchem.2012.10.087"
}
Stanić-Vučinić, D., Prodić, I., Apostolović, D., Nikolić, M.,& Ćirković-Veličković, T.. (2013). Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 138(1), 590-599.
https://doi.org/10.1016/j.foodchem.2012.10.087
Stanić-Vučinić D, Prodić I, Apostolović D, Nikolić M, Ćirković-Veličković T. Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions. in Food Chemistry. 2013;138(1):590-599.
doi:10.1016/j.foodchem.2012.10.087 .
Stanić-Vučinić, Dragana, Prodić, Ivana, Apostolović, Danijela, Nikolić, Milan, Ćirković-Veličković, Tanja, "Structure and antioxidant activity of beta-lactoglobulin-glycoconjugates obtained by high-intensity-ultrasound-induced Maillard reaction in aqueous model systems under neutral conditions" in Food Chemistry, 138, no. 1 (2013):590-599,
https://doi.org/10.1016/j.foodchem.2012.10.087 . .
103
79
113

Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/758
AB  - Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
EP  - 1271
IS  - 3-4
SP  - 1263
VL  - 136
DO  - 10.1016/j.foodchem.2012.09.040
ER  - 
@article{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed",
pages = "1271-1263",
number = "3-4",
volume = "136",
doi = "10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2013). Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. in Food Chemistry
Elsevier Sci Ltd, Oxford., 136(3-4), 1263-1271.
https://doi.org/10.1016/j.foodchem.2012.09.040
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. in Food Chemistry. 2013;136(3-4):1263-1271.
doi:10.1016/j.foodchem.2012.09.040 .
Stojadinović, Marija M., Radosavljević, Jelena, Ognjenović, Jana, Mihailović-Vesić, Jelena, Prodić, Ivana, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed" in Food Chemistry, 136, no. 3-4 (2013):1263-1271,
https://doi.org/10.1016/j.foodchem.2012.09.040 . .
195
135
200

Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis

Ognjenović, Jana; Milčić-Matić, Natalija; Smiljanić, Katarina; Vučković, Olga; Burazer, Lidija; Popović, Nikola; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2013)

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Milčić-Matić, Natalija
AU  - Smiljanić, Katarina
AU  - Vučković, Olga
AU  - Burazer, Lidija
AU  - Popović, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/375
AB  - Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201. (C) 2013 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Veterinary Immunology and Immunopathology
T1  - Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis
EP  - 47
IS  - 1-2
SP  - 38
VL  - 155
DO  - 10.1016/j.vetimm.2013.06.005
ER  - 
@article{
author = "Ognjenović, Jana and Milčić-Matić, Natalija and Smiljanić, Katarina and Vučković, Olga and Burazer, Lidija and Popović, Nikola and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201. (C) 2013 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Veterinary Immunology and Immunopathology",
title = "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis",
pages = "47-38",
number = "1-2",
volume = "155",
doi = "10.1016/j.vetimm.2013.06.005"
}
Ognjenović, J., Milčić-Matić, N., Smiljanić, K., Vučković, O., Burazer, L., Popović, N., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2013). Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology
Elsevier Science Bv, Amsterdam., 155(1-2), 38-47.
https://doi.org/10.1016/j.vetimm.2013.06.005
Ognjenović J, Milčić-Matić N, Smiljanić K, Vučković O, Burazer L, Popović N, Stanić-Vučinić D, Ćirković-Veličković T. Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology. 2013;155(1-2):38-47.
doi:10.1016/j.vetimm.2013.06.005 .
Ognjenović, Jana, Milčić-Matić, Natalija, Smiljanić, Katarina, Vučković, Olga, Burazer, Lidija, Popović, Nikola, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis" in Veterinary Immunology and Immunopathology, 155, no. 1-2 (2013):38-47,
https://doi.org/10.1016/j.vetimm.2013.06.005 . .
14
9
11

Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen

Milčić-Matić, Natalija; Ognjenović, Jana; Burazer, Lidija; Blagojević, Gordan; Popović, Nikola; Lazarević, M.; Stanić-Vučinić, Dragana

(Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd, 2013)

TY  - JOUR
AU  - Milčić-Matić, Natalija
AU  - Ognjenović, Jana
AU  - Burazer, Lidija
AU  - Blagojević, Gordan
AU  - Popović, Nikola
AU  - Lazarević, M.
AU  - Stanić-Vučinić, Dragana
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/370
AB  - Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses.
AB  - Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.
PB  - Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd
T2  - Acta veterinaria - Beograd
T1  - Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen
T1  - Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia
EP  - 451
IS  - 4
SP  - 437
VL  - 63
DO  - 10.2298/AVB1304437M
ER  - 
@article{
author = "Milčić-Matić, Natalija and Ognjenović, Jana and Burazer, Lidija and Blagojević, Gordan and Popović, Nikola and Lazarević, M. and Stanić-Vučinić, Dragana",
year = "2013",
abstract = "Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses., Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.",
publisher = "Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd",
journal = "Acta veterinaria - Beograd",
title = "Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen, Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia",
pages = "451-437",
number = "4",
volume = "63",
doi = "10.2298/AVB1304437M"
}
Milčić-Matić, N., Ognjenović, J., Burazer, L., Blagojević, G., Popović, N., Lazarević, M.,& Stanić-Vučinić, D.. (2013). Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen. in Acta veterinaria - Beograd
Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd., 63(4), 437-451.
https://doi.org/10.2298/AVB1304437M
Milčić-Matić N, Ognjenović J, Burazer L, Blagojević G, Popović N, Lazarević M, Stanić-Vučinić D. Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen. in Acta veterinaria - Beograd. 2013;63(4):437-451.
doi:10.2298/AVB1304437M .
Milčić-Matić, Natalija, Ognjenović, Jana, Burazer, Lidija, Blagojević, Gordan, Popović, Nikola, Lazarević, M., Stanić-Vučinić, Dragana, "Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen" in Acta veterinaria - Beograd, 63, no. 4 (2013):437-451,
https://doi.org/10.2298/AVB1304437M . .
1
1

Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase

Tantoush, Ziyad; Apostolović, Danijela; Kravić, Bojana; Prodić, Ivana; Mihajlovic, Luka; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2012)

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Apostolović, Danijela
AU  - Kravić, Bojana
AU  - Prodić, Ivana
AU  - Mihajlovic, Luka
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/760
AB  - The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Functional Foods
T1  - Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase
EP  - 660
IS  - 3
SP  - 650
VL  - 4
DO  - 10.1016/j.jff.2012.04.006
ER  - 
@article{
author = "Tantoush, Ziyad and Apostolović, Danijela and Kravić, Bojana and Prodić, Ivana and Mihajlovic, Luka and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
abstract = "The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Functional Foods",
title = "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase",
pages = "660-650",
number = "3",
volume = "4",
doi = "10.1016/j.jff.2012.04.006"
}
Tantoush, Z., Apostolović, D., Kravić, B., Prodić, I., Mihajlovic, L., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2012). Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. in Journal of Functional Foods
Elsevier Science Bv, Amsterdam., 4(3), 650-660.
https://doi.org/10.1016/j.jff.2012.04.006
Tantoush Z, Apostolović D, Kravić B, Prodić I, Mihajlovic L, Stanić-Vučinić D, Ćirković-Veličković T. Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. in Journal of Functional Foods. 2012;4(3):650-660.
doi:10.1016/j.jff.2012.04.006 .
Tantoush, Ziyad, Apostolović, Danijela, Kravić, Bojana, Prodić, Ivana, Mihajlovic, Luka, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase" in Journal of Functional Foods, 4, no. 3 (2012):650-660,
https://doi.org/10.1016/j.jff.2012.04.006 . .
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50

One-step method for isolation and purification of native beta-lactoglobulin from bovine whey

Stojadinović, Marija M.; Burazer, Lidija M.; Ercili-Cura, Dilek; Sancho, Ana; Buchert, Johanna; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley-Blackwell, Malden, 2012)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/675
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
EP  - 1440
IS  - 7
SP  - 1432
VL  - 92
DO  - 10.1002/jsfa.4722
ER  - 
@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
pages = "1440-1432",
number = "7",
volume = "92",
doi = "10.1002/jsfa.4722"
}
Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722
Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .
Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .
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