TY  - JOUR
AU  - Prodić, Ivana
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/756
AB  - Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.
PB  - MDPI
T2  - Antioxidants
T1  - Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies
IS  - 4
SP  - 886
VL  - 12
DO  - 10.3390/antiox12040886
ER  - 

@article{
author = "Prodić, Ivana and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.",
publisher = "MDPI",
journal = "Antioxidants",
title = "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies",
number = "4",
pages = "886",
volume = "12",
doi = "10.3390/antiox12040886"
}

Prodić, I., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants
MDPI., 12(4), 886.
https://doi.org/10.3390/antiox12040886

Prodić I, Krstić-Ristivojević M, Smiljanić K. Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants. 2023;12(4):886.
doi:10.3390/antiox12040886 .

Prodić, Ivana, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies" in Antioxidants, 12, no. 4 (2023):886,
https://doi.org/10.3390/antiox12040886 . .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/788
AB  - Food allergies have increased dramatically in the last decade, especially in developedcountries. Food tolerance requires strict maintenance of a specific microbial portfolio inthe gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,which in turn causes inflammation and pathogenic gut conditions leading to thedevelopment of food allergies. Any environmental factors that lead to a disturbanceand/or malfunction of the gastrointestinal tract and digestive performance favor thedevelopment of food allergies.Based on that, what do we know about the role of increasing anthropogenic chemicals,including emerging ones, resulting from the new global situation?There is awareness that their effects are multifaceted, e.g., chemicals affect the growth ofplants and animals and thus the quality of the food produced. In addition, chemicals affectour food during its production and processing, but also affect our body andgastrointestinal tract. It is time to fill the knowledge gaps and understand how theseinteractions between environmental triggers such as industrial and traffic pollution,transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and theirallergenicity, adjuvant effects, and the increasing prevalence of food allergies.Some improvements in this area are already being made through advances in ‘omics’technologies (i.e., proteomics, genomics, metabolomics) and systems biology approachesthat will hopefully provide a scientific understanding of the relationship betweenincreasing food allergies and the increasingly present wide variety of anthropogenicchemicals in our environment.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Food allergies on the rise: the role of anthropogenic chemicals
EP  - 27
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_intor_788
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana",
year = "2023",
abstract = "Food allergies have increased dramatically in the last decade, especially in developedcountries. Food tolerance requires strict maintenance of a specific microbial portfolio inthe gastrointestinal tract, as changes in the gut microbiome can lead to its disruption,which in turn causes inflammation and pathogenic gut conditions leading to thedevelopment of food allergies. Any environmental factors that lead to a disturbanceand/or malfunction of the gastrointestinal tract and digestive performance favor thedevelopment of food allergies.Based on that, what do we know about the role of increasing anthropogenic chemicals,including emerging ones, resulting from the new global situation?There is awareness that their effects are multifaceted, e.g., chemicals affect the growth ofplants and animals and thus the quality of the food produced. In addition, chemicals affectour food during its production and processing, but also affect our body andgastrointestinal tract. It is time to fill the knowledge gaps and understand how theseinteractions between environmental triggers such as industrial and traffic pollution,transition and heavy metals, pesticides, chemtrails, etc., affect food allergens and theirallergenicity, adjuvant effects, and the increasing prevalence of food allergies.Some improvements in this area are already being made through advances in ‘omics’technologies (i.e., proteomics, genomics, metabolomics) and systems biology approachesthat will hopefully provide a scientific understanding of the relationship betweenincreasing food allergies and the increasingly present wide variety of anthropogenicchemicals in our environment.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Food allergies on the rise: the role of anthropogenic chemicals",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_intor_788"
}

Smiljanić, K.,& Prodić, I.. (2023). Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 27-27.
https://hdl.handle.net/21.15107/rcub_intor_788

Smiljanić K, Prodić I. Food allergies on the rise: the role of anthropogenic chemicals. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:27-27.
https://hdl.handle.net/21.15107/rcub_intor_788 .

Smiljanić, Katarina, Prodić, Ivana, "Food allergies on the rise: the role of anthropogenic chemicals" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):27-27,
https://hdl.handle.net/21.15107/rcub_intor_788 .

TY  - CONF
AU  - Protić-Rosić, Isidora
AU  - Lopandić, Zorana
AU  - Popović, Dragan
AU  - Blagojević, Gordan
AU  - Gavrović-Jankulović, Marija
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/714
AB  - Allergen immunotherapy (AIT) is currently the only disease-modifying treatment for
allergies. Pre-clinical models for the evaluation of novel therapeutics are crucial for
ensuring their efficacy and safety. While cell culture models are cost-effective and
efficient, they cannot fully replicate the cellular interactions in vivo. Therefore, it is
essential to use more sophisticated model systems, such as co-cultures, to assess the
potential of new therapeutics more accurately. Immunomodulatory protein banana lectin
(BLwt) is an attractive candidate for adjuvant in AIT. Its mutant BLH84T was developed to
reduce its potential mitogenicity. The aim of this study was the development of the coculture model system for testing the immunomodulatory effect of chimeras composed of
the major birch pollen allergen (Bv1a) and BLwt (Bv1a-BLwt, Cwt), the hypoallergenic
isoform of Bv1a (Bv1l) and BLH84T (Bv1l-BLH84T, C1 and BLH84T-Bv1l, C2). Chimeric
structures were designed in silico, fully minimized, and relaxed without van der Waals
atomic clashes. Afterward, proteins were successfully expressed in Escherichia coli and
purified by IMAC yielding around 0.4 mg per 1L of expression medium. The IgE binding
capacity was assessed using ELISA inhibition with birch pollen allergic patients’ sera.
Caco-2 intestinal epithelial cells and THP-1 differentiated macrophages were used for the
co-culture model system development. After protein application on the apical side of the
co-culture, the integrity of the epithelial monolayer was not disturbed. The
immunomodulatory potential of antigens was tested by measuring the gene expression
levels for pro- and anti-inflammatory cytokines in both cell lines from co-culture. The
obtained results indicate that the best anti-inflammatory response was favored after
treatment with Cwt. Additionally, to further confirm the immunomodulatory effect of the
recombinant chimeras, PBMCs obtained from individuals allergic to birch pollen were
employed and treated with recombinant proteins. Only after treatment with Cwt, PBMCs
secreted the anti-inflammatory cytokine IL-10. Obtained results suggest that Cwt chimera
could have a therapeutic effect in AIT in birch pollen allergy.
PB  - Faculty of Chemistry
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference International scientific meeting September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”
T1  - Evaluation of the immunomodulatory potential of chimera Bv1a-BLwt and its mutants on the co-culture model system
EP  - 72
SP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_intor_714
ER  - 

@conference{
author = "Protić-Rosić, Isidora and Lopandić, Zorana and Popović, Dragan and Blagojević, Gordan and Gavrović-Jankulović, Marija",
year = "2023",
abstract = "Allergen immunotherapy (AIT) is currently the only disease-modifying treatment for
allergies. Pre-clinical models for the evaluation of novel therapeutics are crucial for
ensuring their efficacy and safety. While cell culture models are cost-effective and
efficient, they cannot fully replicate the cellular interactions in vivo. Therefore, it is
essential to use more sophisticated model systems, such as co-cultures, to assess the
potential of new therapeutics more accurately. Immunomodulatory protein banana lectin
(BLwt) is an attractive candidate for adjuvant in AIT. Its mutant BLH84T was developed to
reduce its potential mitogenicity. The aim of this study was the development of the coculture model system for testing the immunomodulatory effect of chimeras composed of
the major birch pollen allergen (Bv1a) and BLwt (Bv1a-BLwt, Cwt), the hypoallergenic
isoform of Bv1a (Bv1l) and BLH84T (Bv1l-BLH84T, C1 and BLH84T-Bv1l, C2). Chimeric
structures were designed in silico, fully minimized, and relaxed without van der Waals
atomic clashes. Afterward, proteins were successfully expressed in Escherichia coli and
purified by IMAC yielding around 0.4 mg per 1L of expression medium. The IgE binding
capacity was assessed using ELISA inhibition with birch pollen allergic patients’ sera.
Caco-2 intestinal epithelial cells and THP-1 differentiated macrophages were used for the
co-culture model system development. After protein application on the apical side of the
co-culture, the integrity of the epithelial monolayer was not disturbed. The
immunomodulatory potential of antigens was tested by measuring the gene expression
levels for pro- and anti-inflammatory cytokines in both cell lines from co-culture. The
obtained results indicate that the best anti-inflammatory response was favored after
treatment with Cwt. Additionally, to further confirm the immunomodulatory effect of the
recombinant chimeras, PBMCs obtained from individuals allergic to birch pollen were
employed and treated with recombinant proteins. Only after treatment with Cwt, PBMCs
secreted the anti-inflammatory cytokine IL-10. Obtained results suggest that Cwt chimera
could have a therapeutic effect in AIT in birch pollen allergy.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference International scientific meeting September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”",
title = "Evaluation of the immunomodulatory potential of chimera Bv1a-BLwt and its mutants on the co-culture model system",
pages = "72-71",
url = "https://hdl.handle.net/21.15107/rcub_intor_714"
}

Protić-Rosić, I., Lopandić, Z., Popović, D., Blagojević, G.,& Gavrović-Jankulović, M.. (2023). Evaluation of the immunomodulatory potential of chimera Bv1a-BLwt and its mutants on the co-culture model system. in Serbian Biochemical Society Twelfth Conference International scientific meeting September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”
Faculty of Chemistry., 71-72.
https://hdl.handle.net/21.15107/rcub_intor_714

Protić-Rosić I, Lopandić Z, Popović D, Blagojević G, Gavrović-Jankulović M. Evaluation of the immunomodulatory potential of chimera Bv1a-BLwt and its mutants on the co-culture model system. in Serbian Biochemical Society Twelfth Conference International scientific meeting September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”. 2023;:71-72.
https://hdl.handle.net/21.15107/rcub_intor_714 .

Protić-Rosić, Isidora, Lopandić, Zorana, Popović, Dragan, Blagojević, Gordan, Gavrović-Jankulović, Marija, "Evaluation of the immunomodulatory potential of chimera Bv1a-BLwt and its mutants on the co-culture model system" in Serbian Biochemical Society Twelfth Conference International scientific meeting September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology” (2023):71-72,
https://hdl.handle.net/21.15107/rcub_intor_714 .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/766
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
DO  - 10.1016/j.foodchem.2022.134981
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
doi = "10.1016/j.foodchem.2022.134981"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/767
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
UR  - https://hdl.handle.net/21.15107/rcub_intor_767
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
url = "https://hdl.handle.net/21.15107/rcub_intor_767"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://hdl.handle.net/21.15107/rcub_intor_767

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
https://hdl.handle.net/21.15107/rcub_intor_767 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://hdl.handle.net/21.15107/rcub_intor_767 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Burazer, Lidija
AU  - Đorić, Nataša
AU  - Krstić-Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/771
AB  - Background and Aim: Epidemiological studies pointed at the connection betweenpollution (e.g., traffic emissions) and an increased percentage of people suffering fromrespiratory allergies, including the pediatric population. Field studies provided the mostrelevant assessment of the effects of the intensity and variety of urban and industrialcontamination on the structure and allergenic potency of pollen allergens. Therefore, theaim of the present work was to compare allergenic profiles ofDactylis glomerata pollen(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assesspollen structures and immunoglobulin E (IgE) reactivity to pollen of school childrenpopulation allergic to grass pollens.
PB  - Udruženje za preventivnu pedijatriju Srbije
C3  - Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
T1  - Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart
EP  - 58
SP  - 58
UR  - https://hdl.handle.net/21.15107/rcub_intor_771
ER  - 

@conference{
author = "Prodić, Ivana and Burazer, Lidija and Đorić, Nataša and Krstić-Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Background and Aim: Epidemiological studies pointed at the connection betweenpollution (e.g., traffic emissions) and an increased percentage of people suffering fromrespiratory allergies, including the pediatric population. Field studies provided the mostrelevant assessment of the effects of the intensity and variety of urban and industrialcontamination on the structure and allergenic potency of pollen allergens. Therefore, theaim of the present work was to compare allergenic profiles ofDactylis glomerata pollen(DGP) collected in the specific urban and rural areas (Kruševac and suburbs), to assesspollen structures and immunoglobulin E (IgE) reactivity to pollen of school childrenpopulation allergic to grass pollens.",
publisher = "Udruženje za preventivnu pedijatriju Srbije",
journal = "Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.",
title = "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart",
pages = "58-58",
url = "https://hdl.handle.net/21.15107/rcub_intor_771"
}

Prodić, I., Burazer, L., Đorić, N., Krstić-Ristivojević, M.,& Smiljanić, K.. (2023). Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.
Udruženje za preventivnu pedijatriju Srbije., 58-58.
https://hdl.handle.net/21.15107/rcub_intor_771

Prodić I, Burazer L, Đorić N, Krstić-Ristivojević M, Smiljanić K. Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart. in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023.. 2023;:58-58.
https://hdl.handle.net/21.15107/rcub_intor_771 .

Prodić, Ivana, Burazer, Lidija, Đorić, Nataša, Krstić-Ristivojević, Maja, Smiljanić, Katarina, "Dactylis glomerata grass pollen from urban area releases more sub- pollen particles and has stronger ige response in allergic individuals than rural counterpart" in Knjiga apstrakata: Deseti nacionalni kongres Udruženja za preventivnu pedijatriju Srbije (UPPS) sa međunarodnim učešćem, Kopaonik, 21-23. april 2023. (2023):58-58,
https://hdl.handle.net/21.15107/rcub_intor_771 .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Ristović, Marina
AU  - Pavlović, Marija
AU  - Nikolić, Stefan
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/635
AB  - The combination of b-oligosaccharides from enzymatically hydrolysed barley b-glucan has attracted interest recently due to its positive effects on human health. This study aimed to assess the impact of the
endo-b-1,3-1,4-glucanase enzyme from Bacillus subtilis 168 on improving the nutritional and bioactive
properties of barley b-glucan. A new procedure for the isolation of b-glucan was developed, at a lower
temperature (45 °C), enabling purity from starch contamination, without affecting the yield (6 g b-glucan
from 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned into E. coli pQE_Ek enables the high
production and purification (82% yield, 1.8 mg mL 1 and 440 U mg 1
) of an enzyme identical to the
natural one (25.5 kDa). The enzymatic reaction showed high efficiency of b-glucan degradation by recombinant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosylD-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacities
by 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicate
the possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barley bglucan used as functional foods.
PB  - Wiley
T2  - International Journal of Food Science and Technology
T1  - Improvement of nutritional and bioactive properties of barley b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase
DO  - 10.1111/ijfs.16647
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Kojić, Milan and Margetić, Aleksandra and Ristović, Marina and Pavlović, Marija and Nikolić, Stefan and Vujčić, Zoran",
year = "2023",
abstract = "The combination of b-oligosaccharides from enzymatically hydrolysed barley b-glucan has attracted interest recently due to its positive effects on human health. This study aimed to assess the impact of the
endo-b-1,3-1,4-glucanase enzyme from Bacillus subtilis 168 on improving the nutritional and bioactive
properties of barley b-glucan. A new procedure for the isolation of b-glucan was developed, at a lower
temperature (45 °C), enabling purity from starch contamination, without affecting the yield (6 g b-glucan
from 100 g of barley flour). The endo-b-1,3-1,4-glucanase is cloned into E. coli pQE_Ek enables the high
production and purification (82% yield, 1.8 mg mL 1 and 440 U mg 1
) of an enzyme identical to the
natural one (25.5 kDa). The enzymatic reaction showed high efficiency of b-glucan degradation by recombinant enzyme, giving a mixture of products (of which 3-O-b-cellobiosyl-D-glucose and 3-O-b-cellotriosylD-glucose are the most abundant), the reduction of viscosity (17%) and increase in antioxidant capacities
by 15.2%, 30.9% and 44.0% assessed by ABTS, DPPH and ORAC, respectively. These results indicate
the possible application of endo-b-1,3-1,4-glucanase enzyme in improving the properties of barley bglucan used as functional foods.",
publisher = "Wiley",
journal = "International Journal of Food Science and Technology",
title = "Improvement of nutritional and bioactive properties of barley b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase",
doi = "10.1111/ijfs.16647"
}

Šokarda Slavić, M., Kojić, M., Margetić, A., Ristović, M., Pavlović, M., Nikolić, S.,& Vujčić, Z.. (2023). Improvement of nutritional and bioactive properties of barley b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology
Wiley..
https://doi.org/10.1111/ijfs.16647

Šokarda Slavić M, Kojić M, Margetić A, Ristović M, Pavlović M, Nikolić S, Vujčić Z. Improvement of nutritional and bioactive properties of barley b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase. in International Journal of Food Science and Technology. 2023;.
doi:10.1111/ijfs.16647 .

Šokarda Slavić, Marinela, Kojić, Milan, Margetić, Aleksandra, Ristović, Marina, Pavlović, Marija, Nikolić, Stefan, Vujčić, Zoran, "Improvement of nutritional and bioactive properties of barley b-glucan-based food products using Bacillus subtilis 168 endo-b-1,3-1,4-glucanase" in International Journal of Food Science and Technology (2023),
https://doi.org/10.1111/ijfs.16647 . .

TY  - JOUR
AU  - Šokarda Slavić, Marinela
AU  - Kojić, Milan
AU  - Margetić, Aleksandra
AU  - Stanisavljević, Nemanja
AU  - Gardijan, Lazar
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/634
AB  - α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications
SP  - 126055
VL  - 249
DO  - 10.1016/j.ijbiomac.2023.126055
ER  - 

@article{
author = "Šokarda Slavić, Marinela and Kojić, Milan and Margetić, Aleksandra and Stanisavljević, Nemanja and Gardijan, Lazar and Božić, Nataša and Vujčić, Zoran",
year = "2023",
abstract = "α-Amylase from the thermophilic bacterial strain Anoxybacillus vranjensis ST4 (AVA) was cloned into the pMALc5HisEk expression vector and successfully expressed and purified from the Escherichia coli ER2523 host strain. AVA belongs to the GH13_5 subfamily of glycoside hydrolases and has 7 conserved sequence regions (CSRs) distributed in three distinct domains (A, B, C). In addition, there is a starch binding domain (SBD) from the CBM20 family of carbohydrate binding modules (CBMs). AVA is a monomer of 66 kDa that achieves maximum activity at 60–80 °C and is active and stable over a wide pH range (4.0–9.0). AVA retained 50 % of its activity after 31 h of incubation at 60 °C and was resistant to a large number of denaturing agents. It hydrolyzed starch granules very efficiently, releasing maltose, maltotriose and maltopentaose as the main products. The hydrolysis rates of raw corn, wheat, horseradish, and potato starch, at a concentration of 10 %, were 87.8, 85.9, 93.0, and 58 %, respectively, at pH 8.5 over a 3 h period. This study showed that the high level of expression as well as the properties of this highly stable and versatile enzyme show all the prerequisites for successful application in industry.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications",
pages = "126055",
volume = "249",
doi = "10.1016/j.ijbiomac.2023.126055"
}

Šokarda Slavić, M., Kojić, M., Margetić, A., Stanisavljević, N., Gardijan, L., Božić, N.,& Vujčić, Z.. (2023). Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules
Elsevier., 249, 126055.
https://doi.org/10.1016/j.ijbiomac.2023.126055

Šokarda Slavić M, Kojić M, Margetić A, Stanisavljević N, Gardijan L, Božić N, Vujčić Z. Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications. in International Journal of Biological Macromolecules. 2023;249:126055.
doi:10.1016/j.ijbiomac.2023.126055 .

Šokarda Slavić, Marinela, Kojić, Milan, Margetić, Aleksandra, Stanisavljević, Nemanja, Gardijan, Lazar, Božić, Nataša, Vujčić, Zoran, "Highly stable and versatile α-amylase from Anoxybacillus vranjensis ST4 suitable for various applications" in International Journal of Biological Macromolecules, 249 (2023):126055,
https://doi.org/10.1016/j.ijbiomac.2023.126055 . .

TY  - JOUR
AU  - Lopandić, Zorana
AU  - Dragačević, Luka
AU  - Kosanović, Dejana
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/787
AB  - In vivo animal models can provide worthy information on various aspects of asthma mechanism and pathogenesis. The genetic predisposition and phenotype of mice may affect the immune response itself. Here we compare the early immune response to Der p 2 or HDM allergen extract upon injection and inhalation in BALB/c and C57BL/6 mice. Female C57BL/6 and BALB/c mice were immunized with Der p 2 allergen subcutaneously followed by inhalation of Der p 2 or HDM extract. After challenge, the mice were euthanized; blood, bronchoalveolar lavage (BAL), spleens and lungs were collected. Cells from BAL were identified by May-Grünwald Giemsa staining and lung leukocyte populations were analyzed by flow cytometry. Serum antibody levels of Der p 2 specific IgE, IgG, IgG1 and IgG2a were assessed by ELISA, and cytokine secretion (IL-4, IFN-γ and IL-10) was evaluated upon stimulation with Der p 2 or HDM extract. The Th2 immune response was confirmed by elevated allergen-specific immunoglobulin E (IgE) and the allergic reaction was evidenced by infiltration of eosinophils and/or neutrophils into BAL. We found that BALB/c mice were inefficient in integrating local with systemic immune response, evidenced by almost no IgG or IgE production upon one subcutaneous injection and subsequent inhalation of Der p 2 allergen; also, the bronchoalveolar lavage infiltrate in these mice consisted of neutrophil infiltration, unlike C57BL/6 mice in which eosinophilic infiltrate predominated. The differences between BALB/c and C57BL/6 mice strains could be exploited for generating different types of responses to the Der p 2 allergen.
PB  - Elsevier
T2  - Journal of Immunological Methods
T2  - Journal of Immunological MethodsJournal of Immunological Methods
T1  - Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols
SP  - 113382
VL  - 511
DO  - 10.1016/j.jim.2022.113382
ER  - 

@article{
author = "Lopandić, Zorana and Dragačević, Luka and Kosanović, Dejana and Burazer, Lidija and Gavrović-Jankulović, Marija and Minić, Rajna",
year = "2022",
abstract = "In vivo animal models can provide worthy information on various aspects of asthma mechanism and pathogenesis. The genetic predisposition and phenotype of mice may affect the immune response itself. Here we compare the early immune response to Der p 2 or HDM allergen extract upon injection and inhalation in BALB/c and C57BL/6 mice. Female C57BL/6 and BALB/c mice were immunized with Der p 2 allergen subcutaneously followed by inhalation of Der p 2 or HDM extract. After challenge, the mice were euthanized; blood, bronchoalveolar lavage (BAL), spleens and lungs were collected. Cells from BAL were identified by May-Grünwald Giemsa staining and lung leukocyte populations were analyzed by flow cytometry. Serum antibody levels of Der p 2 specific IgE, IgG, IgG1 and IgG2a were assessed by ELISA, and cytokine secretion (IL-4, IFN-γ and IL-10) was evaluated upon stimulation with Der p 2 or HDM extract. The Th2 immune response was confirmed by elevated allergen-specific immunoglobulin E (IgE) and the allergic reaction was evidenced by infiltration of eosinophils and/or neutrophils into BAL. We found that BALB/c mice were inefficient in integrating local with systemic immune response, evidenced by almost no IgG or IgE production upon one subcutaneous injection and subsequent inhalation of Der p 2 allergen; also, the bronchoalveolar lavage infiltrate in these mice consisted of neutrophil infiltration, unlike C57BL/6 mice in which eosinophilic infiltrate predominated. The differences between BALB/c and C57BL/6 mice strains could be exploited for generating different types of responses to the Der p 2 allergen.",
publisher = "Elsevier",
journal = "Journal of Immunological Methods, Journal of Immunological MethodsJournal of Immunological Methods",
title = "Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols",
pages = "113382",
volume = "511",
doi = "10.1016/j.jim.2022.113382"
}

Lopandić, Z., Dragačević, L., Kosanović, D., Burazer, L., Gavrović-Jankulović, M.,& Minić, R.. (2022). Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols. in Journal of Immunological Methods
Elsevier., 511, 113382.
https://doi.org/10.1016/j.jim.2022.113382

Lopandić Z, Dragačević L, Kosanović D, Burazer L, Gavrović-Jankulović M, Minić R. Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols. in Journal of Immunological Methods. 2022;511:113382.
doi:10.1016/j.jim.2022.113382 .

Lopandić, Zorana, Dragačević, Luka, Kosanović, Dejana, Burazer, Lidija, Gavrović-Jankulović, Marija, Minić, Rajna, "Differences in mouse strains determine the outcome of Der p 2 allergy induction protocols" in Journal of Immunological Methods, 511 (2022):113382,
https://doi.org/10.1016/j.jim.2022.113382 . .

TY  - JOUR
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Sickmann, Albert
AU  - Solari, Fiorella Andrea
AU  - Kolarević, Stoimir
AU  - Divac Rankov, Aleksandra
AU  - Ljujic, Mila
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/781
AB  - Background: Although still considered a safer alternative to classical cigarettes, growing body of work points toharmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect ofe-cigarettes needs to be investigated in more detail considering their widespread use.Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, withand without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performedvia high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however itnegatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletionin total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteinswere upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data areavailable via ProteomeXchange with identifier PXD032071.Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMsalterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.
PB  - BMC Springer Nature
T2  - Respiratory Research
T1  - Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells
IS  - 191
VL  - 23
DO  - 10.1186/s12931-022-02102-w
ER  - 

@article{
author = "Trifunović, Sara and Smiljanić, Katarina and Sickmann, Albert and Solari, Fiorella Andrea and Kolarević, Stoimir and Divac Rankov, Aleksandra and Ljujic, Mila",
year = "2022",
abstract = "Background: Although still considered a safer alternative to classical cigarettes, growing body of work points toharmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect ofe-cigarettes needs to be investigated in more detail considering their widespread use.Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, withand without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performedvia high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however itnegatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletionin total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteinswere upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data areavailable via ProteomeXchange with identifier PXD032071.Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMsalterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.",
publisher = "BMC Springer Nature",
journal = "Respiratory Research",
title = "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells",
number = "191",
volume = "23",
doi = "10.1186/s12931-022-02102-w"
}

Trifunović, S., Smiljanić, K., Sickmann, A., Solari, F. A., Kolarević, S., Divac Rankov, A.,& Ljujic, M.. (2022). Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research
BMC Springer Nature., 23(191).
https://doi.org/10.1186/s12931-022-02102-w

Trifunović S, Smiljanić K, Sickmann A, Solari FA, Kolarević S, Divac Rankov A, Ljujic M. Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research. 2022;23(191).
doi:10.1186/s12931-022-02102-w .

Trifunović, Sara, Smiljanić, Katarina, Sickmann, Albert, Solari, Fiorella Andrea, Kolarević, Stoimir, Divac Rankov, Aleksandra, Ljujic, Mila, "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells" in Respiratory Research, 23, no. 191 (2022),
https://doi.org/10.1186/s12931-022-02102-w . .

TY  - JOUR
AU  - Lopandic, Zorana
AU  - Dragačević, Luka
AU  - Popovic, Dragan
AU  - Andjelkovic, Uros
AU  - Minić, Rajna
AU  - Gavrovic-Jankulovic, Marija
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/615
AB  - Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms
PB  - MDPI
T2  - Biomolecules
T1  - BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms
IS  - 2
SP  - 180
VL  - 11(2)
VL  - 11
DO  - 10.3390/biom11020180
ER  - 

@article{
author = "Lopandic, Zorana and Dragačević, Luka and Popovic, Dragan and Andjelkovic, Uros and Minić, Rajna and Gavrovic-Jankulovic, Marija",
year = "2021",
abstract = "Fluorescently labeled lectins are useful tools for in vivo and in vitro studies of the structure and function of tissues and various pathogens such as viruses, bacteria, and fungi. For the evaluation of high-mannose glycans present on various glycoproteins, a three-dimensional (3D) model of the chimera was designed from the crystal structures of recombinant banana lectin (BanLec, Protein Data Bank entry (PDB): 5EXG) and an enhanced green fluorescent protein (eGFP, PDB 4EUL) by applying molecular modeling and molecular mechanics and expressed in Escherichia coli. BanLec-eGFP, produced as a soluble cytosolic protein of about 42 kDa, revealed β-sheets (41%) as the predominant secondary structures, with the emission peak maximum detected at 509 nm (excitation wavelength 488 nm). More than 65% of the primary structure was confirmed by mass spectrometry. Competitive BanLec-eGFP binding to high mannose glycans of the influenza vaccine (Vaxigrip®) was shown in a fluorescence-linked lectin sorbent assay (FLLSA) with monosaccharides (mannose and glucose) and wild type BanLec and H84T BanLec mutant. BanLec-eGFP exhibited binding to mannose residues on different strains of Salmonella in flow cytometry, with especially pronounced binding to a Salmonella Typhi clinical isolate. BanLec-eGFP can be a useful tool for screening high-mannose glycosylation sites on different microorganisms",
publisher = "MDPI",
journal = "Biomolecules",
title = "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms",
number = "2",
pages = "180",
volume = "11(2), 11",
doi = "10.3390/biom11020180"
}

Lopandic, Z., Dragačević, L., Popovic, D., Andjelkovic, U., Minić, R.,& Gavrovic-Jankulovic, M.. (2021). BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules
MDPI., 11(2)(2), 180.
https://doi.org/10.3390/biom11020180

Lopandic Z, Dragačević L, Popovic D, Andjelkovic U, Minić R, Gavrovic-Jankulovic M. BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms. in Biomolecules. 2021;11(2)(2):180.
doi:10.3390/biom11020180 .

Lopandic, Zorana, Dragačević, Luka, Popovic, Dragan, Andjelkovic, Uros, Minić, Rajna, Gavrovic-Jankulovic, Marija, "BanLec-eGFP Chimera as a Tool for Evaluation of Lectin Binding to High-Mannose Glycans on Microorganisms" in Biomolecules, 11(2), no. 2 (2021):180,
https://doi.org/10.3390/biom11020180 . .

TY  - JOUR
AU  - Krstić-Ristivojević, Maja
AU  - Apostolović, Danijela
AU  - Smiljanić, Katarina
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/784
AB  - Food hypersensitivity reactions are adverse reactions to harmless dietary substances, whose causes are hidden within derangements of the complex immune machinery of humans and mammals. Until recently, enterocytes were considered as solely absorptive cells providing a physical barrier for unwanted lumen constituents. This review focuses on the enterocytes, which are the hub for innate and adaptive immune reactions. Furthermore, the ambiguous nature of enterocytes is also reflected in the fact that enterocytes can be considered as antigen-presenting cells since they constitutively express major histocompatibility complex (MHC) class II molecules. Taken together, it becomes clear that enterocytes have an immense role in maintaining oral tolerance to foreign antigens. In general, the immune system and its mechanisms underlying food hypersensitivity are still unknown and the involvement of components belonging to other anatomical systems, such as enterocytes, in these mechanisms make their elucidation even more difficult. The findings from studies with animal models provide us with valuable information about allergic mechanisms in the animal world, while on the other hand, these models are used to extrapolate results to the pathological conditions occurring in humans. There is a constant need for studies that deal with this topic and can overcome the glitches related to ethics in working with animals.
PB  - MDPI
T2  - Animals
T1  - Enterocytes in Food Hypersensitivity Reactions
IS  - 9
SP  - 2713
VL  - 11
DO  - 10.3390/ani11092713
ER  - 

@article{
author = "Krstić-Ristivojević, Maja and Apostolović, Danijela and Smiljanić, Katarina",
year = "2021",
abstract = "Food hypersensitivity reactions are adverse reactions to harmless dietary substances, whose causes are hidden within derangements of the complex immune machinery of humans and mammals. Until recently, enterocytes were considered as solely absorptive cells providing a physical barrier for unwanted lumen constituents. This review focuses on the enterocytes, which are the hub for innate and adaptive immune reactions. Furthermore, the ambiguous nature of enterocytes is also reflected in the fact that enterocytes can be considered as antigen-presenting cells since they constitutively express major histocompatibility complex (MHC) class II molecules. Taken together, it becomes clear that enterocytes have an immense role in maintaining oral tolerance to foreign antigens. In general, the immune system and its mechanisms underlying food hypersensitivity are still unknown and the involvement of components belonging to other anatomical systems, such as enterocytes, in these mechanisms make their elucidation even more difficult. The findings from studies with animal models provide us with valuable information about allergic mechanisms in the animal world, while on the other hand, these models are used to extrapolate results to the pathological conditions occurring in humans. There is a constant need for studies that deal with this topic and can overcome the glitches related to ethics in working with animals.",
publisher = "MDPI",
journal = "Animals",
title = "Enterocytes in Food Hypersensitivity Reactions",
number = "9",
pages = "2713",
volume = "11",
doi = "10.3390/ani11092713"
}

Krstić-Ristivojević, M., Apostolović, D.,& Smiljanić, K.. (2021). Enterocytes in Food Hypersensitivity Reactions. in Animals
MDPI., 11(9), 2713.
https://doi.org/10.3390/ani11092713

Krstić-Ristivojević M, Apostolović D, Smiljanić K. Enterocytes in Food Hypersensitivity Reactions. in Animals. 2021;11(9):2713.
doi:10.3390/ani11092713 .

Krstić-Ristivojević, Maja, Apostolović, Danijela, Smiljanić, Katarina, "Enterocytes in Food Hypersensitivity Reactions" in Animals, 11, no. 9 (2021):2713,
https://doi.org/10.3390/ani11092713 . .

TY  - CONF
AU  - Jovanović, Vesna B.
AU  - Smiljanić, Katarina
AU  - Lujić, Tamara
AU  - Đukić, Teodora
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/779
AB  - Edible insects are recommended as a future food because of many reasons. The nutritional value of edible insects is one of criteria for the selection of seven most promising species among which is Tenebrio molitor. The objective of this study was to examine the effects of different flour Tenebrio molitor. Twelve different extraction conditions were set up in which three parameters were combined: pH extraction solutions (6, 8 and 12.5), temperature (30 °C and 60 °C), and ultrasound (US). Shotgun proteomics of trypsin digests profiled protein isolates. The highest protein yield was in extractions at pH 12.5. The temperature elevation and US application significantly increased the yield of isolated proteins at pH 12.5 but their solubility at the pH 7.4 was lower compared to isolates at pH 6 and 8. 1D-SDS-PAGE showed marked differences in protein profiles on various extraction conditions, with highest number of the distinctive bands at pH 8 at 30 °C. Shotgun proteomics showed that extraction condition at pH 12.5, on 30 °C has the highest numbers of different proteins, however, among the top 20 abundant proteins are chitin-associated proteins, allergens and proteinases, while at pH 8 these proteins are not enriched. Highly basic extraction significantly contributes to protein hydrolysis while application of US contributes to the protein cross-linking and this effect is more prominent at high temperatures.
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of extraction conditions on proteins' profiles of Tenebrio molitor
EP  - 53
SP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_intor_779
ER  - 

@conference{
author = "Jovanović, Vesna B. and Smiljanić, Katarina and Lujić, Tamara and Đukić, Teodora and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Edible insects are recommended as a future food because of many reasons. The nutritional value of edible insects is one of criteria for the selection of seven most promising species among which is Tenebrio molitor. The objective of this study was to examine the effects of different flour Tenebrio molitor. Twelve different extraction conditions were set up in which three parameters were combined: pH extraction solutions (6, 8 and 12.5), temperature (30 °C and 60 °C), and ultrasound (US). Shotgun proteomics of trypsin digests profiled protein isolates. The highest protein yield was in extractions at pH 12.5. The temperature elevation and US application significantly increased the yield of isolated proteins at pH 12.5 but their solubility at the pH 7.4 was lower compared to isolates at pH 6 and 8. 1D-SDS-PAGE showed marked differences in protein profiles on various extraction conditions, with highest number of the distinctive bands at pH 8 at 30 °C. Shotgun proteomics showed that extraction condition at pH 12.5, on 30 °C has the highest numbers of different proteins, however, among the top 20 abundant proteins are chitin-associated proteins, allergens and proteinases, while at pH 8 these proteins are not enriched. Highly basic extraction significantly contributes to protein hydrolysis while application of US contributes to the protein cross-linking and this effect is more prominent at high temperatures.",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of extraction conditions on proteins' profiles of Tenebrio molitor",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_intor_779"
}

Jovanović, V. B., Smiljanić, K., Lujić, T., Đukić, T.,& Ćirković-Veličković, T.. (2021). Effects of extraction conditions on proteins' profiles of Tenebrio molitor. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 53-53.
https://hdl.handle.net/21.15107/rcub_intor_779

Jovanović VB, Smiljanić K, Lujić T, Đukić T, Ćirković-Veličković T. Effects of extraction conditions on proteins' profiles of Tenebrio molitor. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:53-53.
https://hdl.handle.net/21.15107/rcub_intor_779 .

Jovanović, Vesna B., Smiljanić, Katarina, Lujić, Tamara, Đukić, Teodora, Ćirković-Veličković, Tanja, "Effects of extraction conditions on proteins' profiles of Tenebrio molitor" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):53-53,
https://hdl.handle.net/21.15107/rcub_intor_779 .

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/780
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting
EP  - 71
SP  - 71
UR  - https://hdl.handle.net/21.15107/rcub_intor_780
ER  - 

@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting",
pages = "71-71",
url = "https://hdl.handle.net/21.15107/rcub_intor_780"
}

Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 71-71.
https://hdl.handle.net/21.15107/rcub_intor_780

Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:71-71.
https://hdl.handle.net/21.15107/rcub_intor_780 .

Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Effects of lysin's and arginige's modifications on trypsin proteolytic efficacy imposed before and after the peanut roasting" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):71-71,
https://hdl.handle.net/21.15107/rcub_intor_780 .

TY  - CONF
AU  - MIhilović, Jelena
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/769
AB  - Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.
C3  - FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia
T1  - Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications
EP  - 27
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_intor_769
ER  - 

@conference{
author = "MIhilović, Jelena and Đukić, Teodora and Smiljanić, Katarina and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.",
journal = "FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia",
title = "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_intor_769"
}

MIhilović, J., Đukić, T., Smiljanić, K., Apostolović, D., Liu, S., Epstein, M. M.,& Ćirković-Veličković, T.. (2021). Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia, 27-27.
https://hdl.handle.net/21.15107/rcub_intor_769

MIhilović J, Đukić T, Smiljanić K, Apostolović D, Liu S, Epstein MM, Ćirković-Veličković T. Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia. 2021;:27-27.
https://hdl.handle.net/21.15107/rcub_intor_769 .

MIhilović, Jelena, Đukić, Teodora, Smiljanić, Katarina, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., Ćirković-Veličković, Tanja, "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications" in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia (2021):27-27,
https://hdl.handle.net/21.15107/rcub_intor_769 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/753
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
EP  - 126
SP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_intor_753
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_intor_753"
}

Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_intor_753

Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_intor_753 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_intor_753 .

TY  - CONF
AU  - Mladenović, Maja
AU  - Romanyuk, Nataliya
AU  - Smiljanić, Katarina
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/773
AB  - Introduction: Shellfish allergy is one of the most common food allergies with a prevalence of 0.5%-2.5% in the general population. The most common allergen present in shellfish is tropomyosin. Detection of tropomyosin in seashells is a challenge because there are no specific antibodies for seashells’ tropomyosin. Our aim was to verify the presence of tropomyosin in Anadara seashells using an immunoproteomic approach and to investigate the level of cross-reactivity with shrimps.Methods and Results: Proteins from lyophilized seashells Tegillarca granosa (TG) and Anadara broughtonii (AB) were extracted in: RIPA buffer (1% Triton X-100, 1% sodium deoxycholate, 0,1% SDS, 150 mM NaCl, 50 mM Tris-HCl, 1mM EDTA) and Rehydration buffer (7M urea, 2M thiourea, 2% CHAPS and 10mM DTT). Protein concentration of extracts was determined by Bradford assay and SDS-PAGE. The presence of tropomyosin has been supported by commercial tropomyosin standard in 1D SDS-PAGE. With 1D immunoblot, it was possible to confirm the reactivity of seashells’ tropomyosin to rabbit anti-shrimp tropomyosin polyclonal antibodies, confirming its presence. Tropomyosin’s presence was also validated with 1D immunoblot using monoclonal antibodies. 2D electrophoresis showed that most of samples’ proteins are in acidic pI range with prevalence of spots in the range 35-50kDa, and, by comparing spots to 2D immunoblot with polyclonal antibodies, it is possible to confirm tropomyosin’s presence in Anadara seashells.Conclusions: We found that tropomyosin is present in both blood clam species. Both monoclonal and polyclonal antibodies raised against shrimp tropomyosin can detect seashells tropomyosin by immunoblot pointing to a potential antibodies cross-reactivity of allergic subjects to shrimps and seashells.
C3  - FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia
T1  - Detection  and characterization of tropomyosin from Anadara Seashells using immunoproteomic aproach
EP  - 35
SP  - 35
UR  - https://hdl.handle.net/21.15107/rcub_intor_773
ER  - 

@conference{
author = "Mladenović, Maja and Romanyuk, Nataliya and Smiljanić, Katarina and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Introduction: Shellfish allergy is one of the most common food allergies with a prevalence of 0.5%-2.5% in the general population. The most common allergen present in shellfish is tropomyosin. Detection of tropomyosin in seashells is a challenge because there are no specific antibodies for seashells’ tropomyosin. Our aim was to verify the presence of tropomyosin in Anadara seashells using an immunoproteomic approach and to investigate the level of cross-reactivity with shrimps.Methods and Results: Proteins from lyophilized seashells Tegillarca granosa (TG) and Anadara broughtonii (AB) were extracted in: RIPA buffer (1% Triton X-100, 1% sodium deoxycholate, 0,1% SDS, 150 mM NaCl, 50 mM Tris-HCl, 1mM EDTA) and Rehydration buffer (7M urea, 2M thiourea, 2% CHAPS and 10mM DTT). Protein concentration of extracts was determined by Bradford assay and SDS-PAGE. The presence of tropomyosin has been supported by commercial tropomyosin standard in 1D SDS-PAGE. With 1D immunoblot, it was possible to confirm the reactivity of seashells’ tropomyosin to rabbit anti-shrimp tropomyosin polyclonal antibodies, confirming its presence. Tropomyosin’s presence was also validated with 1D immunoblot using monoclonal antibodies. 2D electrophoresis showed that most of samples’ proteins are in acidic pI range with prevalence of spots in the range 35-50kDa, and, by comparing spots to 2D immunoblot with polyclonal antibodies, it is possible to confirm tropomyosin’s presence in Anadara seashells.Conclusions: We found that tropomyosin is present in both blood clam species. Both monoclonal and polyclonal antibodies raised against shrimp tropomyosin can detect seashells tropomyosin by immunoblot pointing to a potential antibodies cross-reactivity of allergic subjects to shrimps and seashells.",
journal = "FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia",
title = "Detection  and characterization of tropomyosin from Anadara Seashells using immunoproteomic aproach",
pages = "35-35",
url = "https://hdl.handle.net/21.15107/rcub_intor_773"
}

Mladenović, M., Romanyuk, N., Smiljanić, K., Jovanović, V. B.,& Ćirković-Veličković, T.. (2021). Detection  and characterization of tropomyosin from Anadara Seashells using immunoproteomic aproach. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia, 35-35.
https://hdl.handle.net/21.15107/rcub_intor_773

Mladenović M, Romanyuk N, Smiljanić K, Jovanović VB, Ćirković-Veličković T. Detection  and characterization of tropomyosin from Anadara Seashells using immunoproteomic aproach. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia. 2021;:35-35.
https://hdl.handle.net/21.15107/rcub_intor_773 .

Mladenović, Maja, Romanyuk, Nataliya, Smiljanić, Katarina, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Detection  and characterization of tropomyosin from Anadara Seashells using immunoproteomic aproach" in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia (2021):35-35,
https://hdl.handle.net/21.15107/rcub_intor_773 .

TY  - JOUR
AU  - Protić-Rosić, Isidora
AU  - Nešić, Andrijana
AU  - Lukić, Ivana
AU  - Miljković, Radmila
AU  - Popović, Dragan
AU  - Atanasković-Marković, Marina
AU  - Stojanović, Marijana
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/630
AB  - Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.
PB  - Elsevier
T2  - Molecular Immunology
T1  - Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion
EP  - 67
SP  - 58
VL  - 138
DO  - 10.1016/j.molimm.2021.06.015
ER  - 

@article{
author = "Protić-Rosić, Isidora and Nešić, Andrijana and Lukić, Ivana and Miljković, Radmila and Popović, Dragan and Atanasković-Marković, Marina and Stojanović, Marijana and Gavrović-Jankulović, Marija",
year = "2021",
abstract = "Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.",
publisher = "Elsevier",
journal = "Molecular Immunology",
title = "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion",
pages = "67-58",
volume = "138",
doi = "10.1016/j.molimm.2021.06.015"
}

Protić-Rosić, I., Nešić, A., Lukić, I., Miljković, R., Popović, D., Atanasković-Marković, M., Stojanović, M.,& Gavrović-Jankulović, M.. (2021). Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology
Elsevier., 138, 58-67.
https://doi.org/10.1016/j.molimm.2021.06.015

Protić-Rosić I, Nešić A, Lukić I, Miljković R, Popović D, Atanasković-Marković M, Stojanović M, Gavrović-Jankulović M. Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology. 2021;138:58-67.
doi:10.1016/j.molimm.2021.06.015 .

Protić-Rosić, Isidora, Nešić, Andrijana, Lukić, Ivana, Miljković, Radmila, Popović, Dragan, Atanasković-Marković, Marina, Stojanović, Marijana, Gavrović-Jankulović, Marija, "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion" in Molecular Immunology, 138 (2021):58-67,
https://doi.org/10.1016/j.molimm.2021.06.015 . .

TY  - CHAP
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna B.
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/764
AB  - Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.
PB  - New York : Nova Science Publisher
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications
SP  - 158
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_intor_764
ER  - 

@inbook{
author = "Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna B. and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Post-translational modifications (PTMs) occur in many forms and shapes, widely influencing protein behavior. High-resolution tandem mass spectrometry (HRMS/MS), coupled with dedicated engines for the identification of unspecified PTMs, is a powerful method for their mapping. A majority of proteomic experiments utilize trypsin for digestion, which cleaves the C-terminal peptide bonds of arginine (Arg) and lysine (Lys) amino acids with high catalytic efficiency and selectivity, unless they are followed with proline. At the same time, Arg and Lys residues are frequently modified during food processing by heat and non-thermal treatments, causing oxidation, carbamylation, and various forms of side chain carbonylation, including the other common PTMs (methylation, acetylation, etc.). Consequently, we explored the possibility to re-assess already generated proteomic data (food protein/allergen tryptic peptides) with respect to the possible modulation of the tryptic intestinal digestion pattern caused by PTMs incorporated at Arg and Lys residues. However, most of the proteomic bottom-up experiments are run with porcine trypsin that has been reductively methylated to increase its stability and minimize autoproteolytic effects. Therefore, in this chapter, the utility of the aforementioned idea was explored, by reviewing the differences in structure, affinity, specificity, and catalytic efficiency of trypsin, primarily from porcine, bovine and human species. Porcine trypsin either from pancreas or in recombinant form showed superior performance compared to human and bovine tryptic counterparts. In addition, set of software tools for identification and analyses of PTMs was reviewed with the aim to isolate those capable of in-depth PTMs profiling and their simultaneous relative quantification, such as PEAKS PTM (PEAKS Studio, Bioinformatics Solution Inc., Ontario Canada). Based on our preliminary experimental results, conclusion is that the proposed idea is plausible, because if potential hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just augmented within human intestinal digestion, with respect to inferior performance of human trypsin.",
publisher = "New York : Nova Science Publisher",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications",
pages = "158",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_intor_764"
}

Smiljanić, K., Mihailović, J., Prodić, I., Đukić, T., Vasović, T., Jovanović, V. B.,& Ćirković-Veličković, T.. (2020). Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publisher., 4, 158.
https://hdl.handle.net/21.15107/rcub_intor_764

Smiljanić K, Mihailović J, Prodić I, Đukić T, Vasović T, Jovanović VB, Ćirković-Veličković T. Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;4:158.
https://hdl.handle.net/21.15107/rcub_intor_764 .

Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna B., Ćirković-Veličković, Tanja, "Trypsin as a Proteomic Probe for Assessment of Food Protein Digestibility in Relation to Chemical and Post-translational Modifications" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 4 (2020):158,
https://hdl.handle.net/21.15107/rcub_intor_764 .

TY  - CHAP
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Radosavljević, Jelena
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/765
AB  - Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.
PB  - New York : Nova Science Publishers
T2  - A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
T1  - Food Allergens’ Susceptibility to Proteolysis
SP  - 220
VL  - 6
UR  - https://hdl.handle.net/21.15107/rcub_intor_765
ER  - 

@inbook{
author = "Prodić, Ivana and Smiljanić, Katarina and Radosavljević, Jelena",
year = "2020",
abstract = "Common properties of food allergens are prominent resistance to heat treatment and enzyme proteolysis. Stability of the proteins upon gastrointestinal proteolysis of food highly correlates with its allergenic potential. At this moment, the scientific community is putting a lot of effort to connect the available knowledge on the structure and function of food proteins, with stability to proteolysis in order to provide the most reliable prediction tool for allergenicity of novel proteins. Moreover, choosing the conditions under which gastrointestinal proteolysis is simulated may profoundly affect the results of assays and allergenicity assessment. At the beginning of research, for the link between allergenicity and proteolytic stability, purified allergens were used. However, this approchad was proved to be prone to production of erroneous data, since the proteolytic stability of purified proteins was frequently affected by the methodology used for protein purification and the ratio of protens to digestive enzymes used in the assays. Nowadays, the scientific community thrives to establish in vitro digestion protocols that mimic physiological conditions and take into account complex compositon of the food. New studies support this tendency, since it was shown that the presence of various biomolecules in food matrix affects the proteolysis in the simulated gastrointestinal conditions. On top of that, survival of intact proteins upon proteolysis seems not to be necessary, but frequently protein fragments of higher molecular weight with partially preserved structure might be enough to elicit allergic reaction in sensitized individuals.",
publisher = "New York : Nova Science Publishers",
journal = "A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era",
booktitle = "Food Allergens’ Susceptibility to Proteolysis",
pages = "220",
volume = "6",
url = "https://hdl.handle.net/21.15107/rcub_intor_765"
}

Prodić, I., Smiljanić, K.,& Radosavljević, J.. (2020). Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era
New York : Nova Science Publishers., 6, 220.
https://hdl.handle.net/21.15107/rcub_intor_765

Prodić I, Smiljanić K, Radosavljević J. Food Allergens’ Susceptibility to Proteolysis. in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era. 2020;6:220.
https://hdl.handle.net/21.15107/rcub_intor_765 .

Prodić, Ivana, Smiljanić, Katarina, Radosavljević, Jelena, "Food Allergens’ Susceptibility to Proteolysis" in A Closer Look at Proteolysis: Biochemistry and Molecular Biology in the Post Genomic Era, 6 (2020):220,
https://hdl.handle.net/21.15107/rcub_intor_765 .

TY  - DATA
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/645
AB  - Figure S1-S3:  Figure S1: Digestion of BLG at pH 1.2, 2.5 and 4.0; Figure S2: Digestion of ALA at pH 1.2, 2.5 and 4.0;  Figure S3: MALDI spectra of peptides used in the study Table S1. IgE levels of patients used in the study determined by ImmunoCAP Methods: 1.1 Detection of ALA and BLG by immunoblot; 1.2 Mass spectrometry analysis; 1.3 Size-exclusion chromatography;  1.4 IgG4-binding properties of peptides obtained by digestion; 1.5 Digestion of purified ALA and BLG at different pH; 1.6 MALDI-TOF MS.
PB  - MDPI
T2  - Foods
T1  - Supplementary information for the article: Radosavljević, J.; Apostolović, D.; Mihailović, J.; Atanasković-Marković, M.;  Burazer, L.; van Hage, M.; Ćirković Veličković, T. Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form  Functional Complexes by Aggregation. Foods 2020, 9 (11), 1576. https://doi.org/10.3390/foods9111576.
IS  - 11
VL  - 9
UR  - https://hdl.handle.net/21.15107/rcub_intor_645
ER  - 

@misc{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "Figure S1-S3:  Figure S1: Digestion of BLG at pH 1.2, 2.5 and 4.0; Figure S2: Digestion of ALA at pH 1.2, 2.5 and 4.0;  Figure S3: MALDI spectra of peptides used in the study Table S1. IgE levels of patients used in the study determined by ImmunoCAP Methods: 1.1 Detection of ALA and BLG by immunoblot; 1.2 Mass spectrometry analysis; 1.3 Size-exclusion chromatography;  1.4 IgG4-binding properties of peptides obtained by digestion; 1.5 Digestion of purified ALA and BLG at different pH; 1.6 MALDI-TOF MS.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary information for the article: Radosavljević, J.; Apostolović, D.; Mihailović, J.; Atanasković-Marković, M.;  Burazer, L.; van Hage, M.; Ćirković Veličković, T. Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form  Functional Complexes by Aggregation. Foods 2020, 9 (11), 1576. https://doi.org/10.3390/foods9111576.",
number = "11",
volume = "9",
url = "https://hdl.handle.net/21.15107/rcub_intor_645"
}

Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2020). Supplementary information for the article: Radosavljević, J.; Apostolović, D.; Mihailović, J.; Atanasković-Marković, M.;  Burazer, L.; van Hage, M.; Ćirković Veličković, T. Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form  Functional Complexes by Aggregation. Foods 2020, 9 (11), 1576. https://doi.org/10.3390/foods9111576.. in Foods
MDPI., 9(11).
https://hdl.handle.net/21.15107/rcub_intor_645

Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Supplementary information for the article: Radosavljević, J.; Apostolović, D.; Mihailović, J.; Atanasković-Marković, M.;  Burazer, L.; van Hage, M.; Ćirković Veličković, T. Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form  Functional Complexes by Aggregation. Foods 2020, 9 (11), 1576. https://doi.org/10.3390/foods9111576.. in Foods. 2020;9(11).
https://hdl.handle.net/21.15107/rcub_intor_645 .

Radosavljević, Jelena, Apostolović, Danijela, Mihailović, Jelena, Atanasković-Marković, Marina, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Supplementary information for the article: Radosavljević, J.; Apostolović, D.; Mihailović, J.; Atanasković-Marković, M.;  Burazer, L.; van Hage, M.; Ćirković Veličković, T. Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form  Functional Complexes by Aggregation. Foods 2020, 9 (11), 1576. https://doi.org/10.3390/foods9111576." in Foods, 9, no. 11 (2020),
https://hdl.handle.net/21.15107/rcub_intor_645 .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/547
AB  - The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.
PB  - MDPI, Basel
T2  - Foods
T1  - Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation
IS  - 11
VL  - 9
DO  - 10.3390/foods9111576
ER  - 

@article{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.",
publisher = "MDPI, Basel",
journal = "Foods",
title = "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation",
number = "11",
volume = "9",
doi = "10.3390/foods9111576"
}

Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2020). Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods
MDPI, Basel., 9(11).
https://doi.org/10.3390/foods9111576

Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods. 2020;9(11).
doi:10.3390/foods9111576 .

Radosavljević, Jelena, Apostolović, Danijela, Mihailović, Jelena, Atanasković-Marković, Marina, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation" in Foods, 9, no. 11 (2020),
https://doi.org/10.3390/foods9111576 . .

TY  - DATA
AU  - Stojanović, Marijana
AU  - Lukić, Ivana
AU  - Marinković, Emilija
AU  - Kovačević, Ana
AU  - Miljković, Radmila
AU  - Tobias, Joshua
AU  - Schabussova, Irma
AU  - Zlatović, Mario
AU  - Barisani-Asenbauer, Talin
AU  - Wiedermann, Ursula
AU  - Inić-Kanada, Aleksandra
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/643
AB  - Table S1: Characteristics of selected anti-tetanus mAbs [35,36].
PB  - MDPI
T2  - Vaccines
T1  - Supplementary information for the article: Stojanović, M.; Lukić, I.; Marinković, E.; Kovačević, A.; Miljković, R.; Tobias, J.; Schabussova, I.; Zlatović, M.; Barisani-Asenbauer, T.; Wiedermann, U.; Inić-Kanada, A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. Vaccines 2020, 8 (4), 719. https://doi.org/10.3390/vaccines8040719.
IS  - 4
SP  - 719
VL  - 8
UR  - https://hdl.handle.net/21.15107/rcub_intor_643
ER  - 

@misc{
author = "Stojanović, Marijana and Lukić, Ivana and Marinković, Emilija and Kovačević, Ana and Miljković, Radmila and Tobias, Joshua and Schabussova, Irma and Zlatović, Mario and Barisani-Asenbauer, Talin and Wiedermann, Ursula and Inić-Kanada, Aleksandra",
year = "2020",
abstract = "Table S1: Characteristics of selected anti-tetanus mAbs [35,36].",
publisher = "MDPI",
journal = "Vaccines",
title = "Supplementary information for the article: Stojanović, M.; Lukić, I.; Marinković, E.; Kovačević, A.; Miljković, R.; Tobias, J.; Schabussova, I.; Zlatović, M.; Barisani-Asenbauer, T.; Wiedermann, U.; Inić-Kanada, A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. Vaccines 2020, 8 (4), 719. https://doi.org/10.3390/vaccines8040719.",
number = "4",
pages = "719",
volume = "8",
url = "https://hdl.handle.net/21.15107/rcub_intor_643"
}

Stojanović, M., Lukić, I., Marinković, E., Kovačević, A., Miljković, R., Tobias, J., Schabussova, I., Zlatović, M., Barisani-Asenbauer, T., Wiedermann, U.,& Inić-Kanada, A.. (2020). Supplementary information for the article: Stojanović, M.; Lukić, I.; Marinković, E.; Kovačević, A.; Miljković, R.; Tobias, J.; Schabussova, I.; Zlatović, M.; Barisani-Asenbauer, T.; Wiedermann, U.; Inić-Kanada, A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. Vaccines 2020, 8 (4), 719. https://doi.org/10.3390/vaccines8040719.. in Vaccines
MDPI., 8(4), 719.
https://hdl.handle.net/21.15107/rcub_intor_643

Stojanović M, Lukić I, Marinković E, Kovačević A, Miljković R, Tobias J, Schabussova I, Zlatović M, Barisani-Asenbauer T, Wiedermann U, Inić-Kanada A. Supplementary information for the article: Stojanović, M.; Lukić, I.; Marinković, E.; Kovačević, A.; Miljković, R.; Tobias, J.; Schabussova, I.; Zlatović, M.; Barisani-Asenbauer, T.; Wiedermann, U.; Inić-Kanada, A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. Vaccines 2020, 8 (4), 719. https://doi.org/10.3390/vaccines8040719.. in Vaccines. 2020;8(4):719.
https://hdl.handle.net/21.15107/rcub_intor_643 .

Stojanović, Marijana, Lukić, Ivana, Marinković, Emilija, Kovačević, Ana, Miljković, Radmila, Tobias, Joshua, Schabussova, Irma, Zlatović, Mario, Barisani-Asenbauer, Talin, Wiedermann, Ursula, Inić-Kanada, Aleksandra, "Supplementary information for the article: Stojanović, M.; Lukić, I.; Marinković, E.; Kovačević, A.; Miljković, R.; Tobias, J.; Schabussova, I.; Zlatović, M.; Barisani-Asenbauer, T.; Wiedermann, U.; Inić-Kanada, A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. Vaccines 2020, 8 (4), 719. https://doi.org/10.3390/vaccines8040719." in Vaccines, 8, no. 4 (2020):719,
https://hdl.handle.net/21.15107/rcub_intor_643 .

TY  - JOUR
AU  - Stojanović, Marijana
AU  - Lukić, Ivana
AU  - Marinković, Emilija
AU  - Kovačević, Ana
AU  - Miljković, Radmila
AU  - Tobias, Joshua
AU  - Schabussova, Irma
AU  - Zlatović, Mario
AU  - Barisani-Asenbauer, Talin
AU  - Wiedermann, Ursula
AU  - Inić-Kanada, Aleksandra
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/552
AB  - Vaccines can have heterologous effects on the immune system, i.e., effects other than triggering an immune response against the disease targeted by the vaccine. We investigated whether monoclonal antibodies (mAbs) specific for tetanus could cross-react with Chlamydia and confer heterologous protection against chlamydial infection. The capability of two tetanus-specific mAbs, namely mAb26 and mAb51, to prevent chlamydial infection has been assessed: (i) in vitro, by performing a neutralization assay using human conjunctival epithelial (HCjE) cells infected with Chlamydia trachomatis serovar B, and (ii) in vivo, by using a guinea pig model of Chlamydia caviae-induced inclusion conjunctivitis. The mAb26 has been superior in comparison with mAb51 in the prevention of chlamydial infection in HCjE cells. The mAb26 has conferred approximate to 40% inhibition of the infection, compared to less than 5% inhibition in the presence of the mAb51. In vivo, mAb26 significantly diminished ocular pathology intensity in guinea pigs infected with C. caviae compared to either the mAb51-treated or sham-treated guinea pigs. Our data provide insights that tetanus immunization generates antibodies which induce heterologous chlamydial immunity and promote protection beyond the intended target pathogen.
PB  - MDPI, Basel
T2  - Vaccines
T1  - Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia
IS  - 4
SP  - 719
VL  - 8
DO  - 10.3390/vaccines8040719
ER  - 

@article{
author = "Stojanović, Marijana and Lukić, Ivana and Marinković, Emilija and Kovačević, Ana and Miljković, Radmila and Tobias, Joshua and Schabussova, Irma and Zlatović, Mario and Barisani-Asenbauer, Talin and Wiedermann, Ursula and Inić-Kanada, Aleksandra",
year = "2020",
abstract = "Vaccines can have heterologous effects on the immune system, i.e., effects other than triggering an immune response against the disease targeted by the vaccine. We investigated whether monoclonal antibodies (mAbs) specific for tetanus could cross-react with Chlamydia and confer heterologous protection against chlamydial infection. The capability of two tetanus-specific mAbs, namely mAb26 and mAb51, to prevent chlamydial infection has been assessed: (i) in vitro, by performing a neutralization assay using human conjunctival epithelial (HCjE) cells infected with Chlamydia trachomatis serovar B, and (ii) in vivo, by using a guinea pig model of Chlamydia caviae-induced inclusion conjunctivitis. The mAb26 has been superior in comparison with mAb51 in the prevention of chlamydial infection in HCjE cells. The mAb26 has conferred approximate to 40% inhibition of the infection, compared to less than 5% inhibition in the presence of the mAb51. In vivo, mAb26 significantly diminished ocular pathology intensity in guinea pigs infected with C. caviae compared to either the mAb51-treated or sham-treated guinea pigs. Our data provide insights that tetanus immunization generates antibodies which induce heterologous chlamydial immunity and promote protection beyond the intended target pathogen.",
publisher = "MDPI, Basel",
journal = "Vaccines",
title = "Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia",
number = "4",
pages = "719",
volume = "8",
doi = "10.3390/vaccines8040719"
}

Stojanović, M., Lukić, I., Marinković, E., Kovačević, A., Miljković, R., Tobias, J., Schabussova, I., Zlatović, M., Barisani-Asenbauer, T., Wiedermann, U.,& Inić-Kanada, A.. (2020). Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. in Vaccines
MDPI, Basel., 8(4), 719.
https://doi.org/10.3390/vaccines8040719

Stojanović M, Lukić I, Marinković E, Kovačević A, Miljković R, Tobias J, Schabussova I, Zlatović M, Barisani-Asenbauer T, Wiedermann U, Inić-Kanada A. Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia. in Vaccines. 2020;8(4):719.
doi:10.3390/vaccines8040719 .

Stojanović, Marijana, Lukić, Ivana, Marinković, Emilija, Kovačević, Ana, Miljković, Radmila, Tobias, Joshua, Schabussova, Irma, Zlatović, Mario, Barisani-Asenbauer, Talin, Wiedermann, Ursula, Inić-Kanada, Aleksandra, "Cross-Reactive Effects of Vaccines: Heterologous Immunity between Tetanus and Chlamydia" in Vaccines, 8, no. 4 (2020):719,
https://doi.org/10.3390/vaccines8040719 . .

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 .