Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research

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Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (en)
Authors

Publications

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 .

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 . .
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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 . .
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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 . .
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33

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
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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

Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Burazer, Lidija; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Elsevier Ltd, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/388
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.
PB  - Elsevier Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
EP  - 59
SP  - 53
VL  - 94
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.",
publisher = "Elsevier Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
pages = "59-53",
volume = "94",
doi = "10.1016/j.phytochem.2013.06.006"
}
Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Elsevier Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006
Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .
Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .
1
18
16
19

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

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 . .
49
41
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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One-step method for isolation and purification of native beta-lactoglobulin from bovine whey

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

(Wiley-Blackwell, Malden, 2012)

TY  - JOUR
AU  - Stojadinović, Marija
AU  - Burazer, Lidija
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/123456789/361
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 and Burazer, Lidija 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., Burazer, L., 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 M, Burazer L, 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, Burazer, Lidija, 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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