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 . .