TY  - DATA
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3020
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4
VL  - 7
IS  - 1
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3020
ER  - 

@misc{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4",
volume = "7",
number = "1",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3020"
}

Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2017). Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4. in Scientific Reports
Nature Publishing Group, London., 7(1).
https://hdl.handle.net/21.15107/rcub_cherry_3020

Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4. in Scientific Reports. 2017;7(1).
https://hdl.handle.net/21.15107/rcub_cherry_3020 .

Apostolović, Danijela, Krstić-Ristivojević, Maja, Mihailović-Vesić, Jelena, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4" in Scientific Reports, 7, no. 1 (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3020 .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2486
AB  - The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides
VL  - 7
DO  - 10.1038/s41598-017-05355-4
ER  - 

@article{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
abstract = "The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides",
volume = "7",
doi = "10.1038/s41598-017-05355-4"
}

Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2017). Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides. in Scientific Reports
Nature Publishing Group, London., 7.
https://doi.org/10.1038/s41598-017-05355-4

Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides. in Scientific Reports. 2017;7.
doi:10.1038/s41598-017-05355-4 .

Apostolović, Danijela, Krstić-Ristivojević, Maja, Mihailović-Vesić, Jelena, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides" in Scientific Reports, 7 (2017),
https://doi.org/10.1038/s41598-017-05355-4 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Mihajlovic, Luka
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1510
AB  - ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy
VL  - 58
IS  - 3
SP  - 635
EP  - 646
DO  - 10.1002/mnfr.201300403
ER  - 

@article{
author = "Radosavljević, Jelena and Nordlund, Emilia and Mihajlovic, Luka and Krstić-Ristivojević, Maja and Bohn, Torsten and Buchert, Johanna and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2014",
abstract = "ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy",
volume = "58",
number = "3",
pages = "635-646",
doi = "10.1002/mnfr.201300403"
}

Radosavljević, J., Nordlund, E., Mihajlovic, L., Krstić-Ristivojević, M., Bohn, T., Buchert, J., Ćirković-Veličković, T.,& Smit, J.. (2014). Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. in Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 58(3), 635-646.
https://doi.org/10.1002/mnfr.201300403

Radosavljević J, Nordlund E, Mihajlovic L, Krstić-Ristivojević M, Bohn T, Buchert J, Ćirković-Veličković T, Smit J. Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. in Molecular Nutrition and Food Research. 2014;58(3):635-646.
doi:10.1002/mnfr.201300403 .

Radosavljević, Jelena, Nordlund, Emilia, Mihajlovic, Luka, Krstić-Ristivojević, Maja, Bohn, Torsten, Buchert, Johanna, Ćirković-Veličković, Tanja, Smit, Joost, "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy" in Molecular Nutrition and Food Research, 58, no. 3 (2014):635-646,
https://doi.org/10.1002/mnfr.201300403 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Waden, Konrad
AU  - Binnmyr, J.
AU  - Hamsten, Carl
AU  - Gronneberg, R.
AU  - Palmberg, C.
AU  - Milčić-Matić, Natalija
AU  - Bergman, T.
AU  - Gronlund, Hans
AU  - van Hage, Marianne
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1634
AB  - Background Allergy to dog (Canis familiaris) is a worldwide common cause of asthma and allergic rhinitis. However, dander extract in routine diagnostics is not an optimal predictor of IgE-mediated dog allergy. Our objective was to evaluate saliva as an allergen source for improved diagnostics of allergy to dog. Methods IgE-binding proteins in dog saliva and dander extract were analysed by immunoblot and mass spectrometry (LC-MS/MS) using pooled or individual sera from dog-allergic patients (n=13). Sera from 59 patients IgE positive to dander and 55 patients IgE negative to dander but with symptoms to dog were analysed for IgE against saliva and dander by ELISA. Basophil stimulation with dog saliva and dander extract was measured by flow cytometry among three dog-allergic patients. Additionally, IgE-binding protein profiles of saliva from different breeds were investigated by immunoblot. Results Greater number and diversity of IgE-binding proteins was found in saliva compared to dander extract and varied among dog breeds. In saliva, Can f 1, 2, 3 and 6 were identified but also four new saliva allergen candidates. The majority of the 59 dog danderpositive sera (n=44) were IgE positive to dog saliva. Among patients IgE negative to dander, but with symptoms to dog, 20% were IgE positive to saliva. The biological activity of saliva was confirmed by basophil degranulation. Conclusions Dog saliva is an allergen source for improved diagnostics of dog allergy. The IgE-binding protein profile of saliva from different dogs varies.
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - Dog saliva - an important source of dog allergens
VL  - 68
IS  - 5
SP  - 585
EP  - 592
DO  - 10.1111/all.12130
ER  - 

@article{
author = "Polović, Natalija and Waden, Konrad and Binnmyr, J. and Hamsten, Carl and Gronneberg, R. and Palmberg, C. and Milčić-Matić, Natalija and Bergman, T. and Gronlund, Hans and van Hage, Marianne",
year = "2013",
abstract = "Background Allergy to dog (Canis familiaris) is a worldwide common cause of asthma and allergic rhinitis. However, dander extract in routine diagnostics is not an optimal predictor of IgE-mediated dog allergy. Our objective was to evaluate saliva as an allergen source for improved diagnostics of allergy to dog. Methods IgE-binding proteins in dog saliva and dander extract were analysed by immunoblot and mass spectrometry (LC-MS/MS) using pooled or individual sera from dog-allergic patients (n=13). Sera from 59 patients IgE positive to dander and 55 patients IgE negative to dander but with symptoms to dog were analysed for IgE against saliva and dander by ELISA. Basophil stimulation with dog saliva and dander extract was measured by flow cytometry among three dog-allergic patients. Additionally, IgE-binding protein profiles of saliva from different breeds were investigated by immunoblot. Results Greater number and diversity of IgE-binding proteins was found in saliva compared to dander extract and varied among dog breeds. In saliva, Can f 1, 2, 3 and 6 were identified but also four new saliva allergen candidates. The majority of the 59 dog danderpositive sera (n=44) were IgE positive to dog saliva. Among patients IgE negative to dander, but with symptoms to dog, 20% were IgE positive to saliva. The biological activity of saliva was confirmed by basophil degranulation. Conclusions Dog saliva is an allergen source for improved diagnostics of dog allergy. The IgE-binding protein profile of saliva from different dogs varies.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Dog saliva - an important source of dog allergens",
volume = "68",
number = "5",
pages = "585-592",
doi = "10.1111/all.12130"
}

Polović, N., Waden, K., Binnmyr, J., Hamsten, C., Gronneberg, R., Palmberg, C., Milčić-Matić, N., Bergman, T., Gronlund, H.,& van Hage, M.. (2013). Dog saliva - an important source of dog allergens. in Allergy
Wiley-Blackwell, Hoboken., 68(5), 585-592.
https://doi.org/10.1111/all.12130

Polović N, Waden K, Binnmyr J, Hamsten C, Gronneberg R, Palmberg C, Milčić-Matić N, Bergman T, Gronlund H, van Hage M. Dog saliva - an important source of dog allergens. in Allergy. 2013;68(5):585-592.
doi:10.1111/all.12130 .

Polović, Natalija, Waden, Konrad, Binnmyr, J., Hamsten, Carl, Gronneberg, R., Palmberg, C., Milčić-Matić, Natalija, Bergman, T., Gronlund, Hans, van Hage, Marianne, "Dog saliva - an important source of dog allergens" in Allergy, 68, no. 5 (2013):585-592,
https://doi.org/10.1111/all.12130 . .

TY  - DATA
AU  - Polović, Natalija
AU  - Waden, Konrad
AU  - Binnmyr, J.
AU  - Hamsten, Carl
AU  - Gronneberg, R.
AU  - Palmberg, C.
AU  - Milčić-Matić, Natalija
AU  - Bergman, T.
AU  - Gronlund, Hans
AU  - van Hage, Marianne
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3488
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - Supplementary data for article: Polović, N.; Waden, K.; Binnmyr, J.; Hamsten, C.; Gronneberg, R.; Palmberg, C.; Milčić-Matić, N.; Bergman, T.; Gronlund, H.; van Hage, M. Dog Saliva - an Important Source of Dog Allergens. Allergy 2013, 68 (5), 585–592. https://doi.org/10.1111/all.12130
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3488
ER  - 

@misc{
author = "Polović, Natalija and Waden, Konrad and Binnmyr, J. and Hamsten, Carl and Gronneberg, R. and Palmberg, C. and Milčić-Matić, Natalija and Bergman, T. and Gronlund, Hans and van Hage, Marianne",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Supplementary data for article: Polović, N.; Waden, K.; Binnmyr, J.; Hamsten, C.; Gronneberg, R.; Palmberg, C.; Milčić-Matić, N.; Bergman, T.; Gronlund, H.; van Hage, M. Dog Saliva - an Important Source of Dog Allergens. Allergy 2013, 68 (5), 585–592. https://doi.org/10.1111/all.12130",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3488"
}

Polović, N., Waden, K., Binnmyr, J., Hamsten, C., Gronneberg, R., Palmberg, C., Milčić-Matić, N., Bergman, T., Gronlund, H.,& van Hage, M.. (2013). Supplementary data for article: Polović, N.; Waden, K.; Binnmyr, J.; Hamsten, C.; Gronneberg, R.; Palmberg, C.; Milčić-Matić, N.; Bergman, T.; Gronlund, H.; van Hage, M. Dog Saliva - an Important Source of Dog Allergens. Allergy 2013, 68 (5), 585–592. https://doi.org/10.1111/all.12130. in Allergy
Wiley-Blackwell, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3488

Polović N, Waden K, Binnmyr J, Hamsten C, Gronneberg R, Palmberg C, Milčić-Matić N, Bergman T, Gronlund H, van Hage M. Supplementary data for article: Polović, N.; Waden, K.; Binnmyr, J.; Hamsten, C.; Gronneberg, R.; Palmberg, C.; Milčić-Matić, N.; Bergman, T.; Gronlund, H.; van Hage, M. Dog Saliva - an Important Source of Dog Allergens. Allergy 2013, 68 (5), 585–592. https://doi.org/10.1111/all.12130. in Allergy. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3488 .

Polović, Natalija, Waden, Konrad, Binnmyr, J., Hamsten, Carl, Gronneberg, R., Palmberg, C., Milčić-Matić, Natalija, Bergman, T., Gronlund, Hans, van Hage, Marianne, "Supplementary data for article: Polović, N.; Waden, K.; Binnmyr, J.; Hamsten, C.; Gronneberg, R.; Palmberg, C.; Milčić-Matić, N.; Bergman, T.; Gronlund, H.; van Hage, M. Dog Saliva - an Important Source of Dog Allergens. Allergy 2013, 68 (5), 585–592. https://doi.org/10.1111/all.12130" in Allergy (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3488 .