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  - Apostolović, Danijela
AU  - Sanchez-Vidaurre, Sara
AU  - Waden, Konrad
AU  - Curin, Mirela
AU  - Grundström, Jeanette
AU  - Gafvelin, Guro
AU  - Ćirković-Veličković, Tanja
AU  - Gronlund, Hans
AU  - Thomas, Wayne R.
AU  - Valenta, Rudolf
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3650
AB  - We investigated the prevalence of sensitization to the cat lipocalin Fel d 7 among 140 cat-sensitized Swedish patients and elucidated its allergenic activity and cross-reactivity with the dog lipocalin Can f 1. Sixty-five of 140 patients had IgE to rFel d 7 whereof 60 also had IgE to rCan f 1. A moderate correlation between IgE levels to rFel d 7 and rCan f 1 was found. rFel d 7 activated basophils in vitro and inhibited IgE binding to rCan f 1 in 4 of 13 patients, whereas rCan f 1 inhibited IgE binding to rFel d 7 in 7 of 13 patients. Fel d 7 and Can f 1 showed high similarities in protein structure and epitopes in common were found using cross-reactive antisera. Fel d 7 is a common allergen in a Swedish cat-sensitized population that cross-reacts with Can f 1, and may contribute to symptoms in cat-but also in dog-allergic patients.
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1
VL  - 71
IS  - 10
SP  - 1490
EP  - 1495
DO  - 10.1111/all.12955
ER  - 

@article{
author = "Apostolović, Danijela and Sanchez-Vidaurre, Sara and Waden, Konrad and Curin, Mirela and Grundström, Jeanette and Gafvelin, Guro and Ćirković-Veličković, Tanja and Gronlund, Hans and Thomas, Wayne R. and Valenta, Rudolf and Hamsten, Carl and van Hage, Marianne",
year = "2016",
abstract = "We investigated the prevalence of sensitization to the cat lipocalin Fel d 7 among 140 cat-sensitized Swedish patients and elucidated its allergenic activity and cross-reactivity with the dog lipocalin Can f 1. Sixty-five of 140 patients had IgE to rFel d 7 whereof 60 also had IgE to rCan f 1. A moderate correlation between IgE levels to rFel d 7 and rCan f 1 was found. rFel d 7 activated basophils in vitro and inhibited IgE binding to rCan f 1 in 4 of 13 patients, whereas rCan f 1 inhibited IgE binding to rFel d 7 in 7 of 13 patients. Fel d 7 and Can f 1 showed high similarities in protein structure and epitopes in common were found using cross-reactive antisera. Fel d 7 is a common allergen in a Swedish cat-sensitized population that cross-reacts with Can f 1, and may contribute to symptoms in cat-but also in dog-allergic patients.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1",
volume = "71",
number = "10",
pages = "1490-1495",
doi = "10.1111/all.12955"
}

Apostolović, D., Sanchez-Vidaurre, S., Waden, K., Curin, M., Grundström, J., Gafvelin, G., Ćirković-Veličković, T., Gronlund, H., Thomas, W. R., Valenta, R., Hamsten, C.,& van Hage, M.. (2016). The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. in Allergy
Wiley-Blackwell, Hoboken., 71(10), 1490-1495.
https://doi.org/10.1111/all.12955

Apostolović D, Sanchez-Vidaurre S, Waden K, Curin M, Grundström J, Gafvelin G, Ćirković-Veličković T, Gronlund H, Thomas WR, Valenta R, Hamsten C, van Hage M. The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. in Allergy. 2016;71(10):1490-1495.
doi:10.1111/all.12955 .

Apostolović, Danijela, Sanchez-Vidaurre, Sara, Waden, Konrad, Curin, Mirela, Grundström, Jeanette, Gafvelin, Guro, Ćirković-Veličković, Tanja, Gronlund, Hans, Thomas, Wayne R., Valenta, Rudolf, Hamsten, Carl, van Hage, Marianne, "The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1" in Allergy, 71, no. 10 (2016):1490-1495,
https://doi.org/10.1111/all.12955 . .

TY  - DATA
AU  - Apostolović, Danijela
AU  - Sanchez-Vidaurre, Sara
AU  - Waden, Konrad
AU  - Curin, Mirela
AU  - Grundström, Jeanette
AU  - Gafvelin, Guro
AU  - Ćirković-Veličković, Tanja
AU  - Gronlund, Hans
AU  - Thomas, Wayne R.
AU  - Valenta, Rudolf
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3651
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - Supplementary data for the article: Apostolovic, D.; Sánchez-Vidaurre, S.; Waden, K.; Curin, M.; Grundström, J.; Gafvelin, G.; Cirkovic Velickovic, T.; Grönlund, H.; Thomas, W. R.; Valenta, R.; et al. The Cat Lipocalin Fel d 7 and Its Cross-Reactivity with the Dog Lipocalin Can f 1. Allergy: European Journal of Allergy and Clinical Immunology 2016, 71 (10), 1490–1495. https://doi.org/10.1111/all.12955
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3651
ER  - 

@misc{
author = "Apostolović, Danijela and Sanchez-Vidaurre, Sara and Waden, Konrad and Curin, Mirela and Grundström, Jeanette and Gafvelin, Guro and Ćirković-Veličković, Tanja and Gronlund, Hans and Thomas, Wayne R. and Valenta, Rudolf and Hamsten, Carl and van Hage, Marianne",
year = "2016",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Supplementary data for the article: Apostolovic, D.; Sánchez-Vidaurre, S.; Waden, K.; Curin, M.; Grundström, J.; Gafvelin, G.; Cirkovic Velickovic, T.; Grönlund, H.; Thomas, W. R.; Valenta, R.; et al. The Cat Lipocalin Fel d 7 and Its Cross-Reactivity with the Dog Lipocalin Can f 1. Allergy: European Journal of Allergy and Clinical Immunology 2016, 71 (10), 1490–1495. https://doi.org/10.1111/all.12955",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3651"
}

Apostolović, D., Sanchez-Vidaurre, S., Waden, K., Curin, M., Grundström, J., Gafvelin, G., Ćirković-Veličković, T., Gronlund, H., Thomas, W. R., Valenta, R., Hamsten, C.,& van Hage, M.. (2016). Supplementary data for the article: Apostolovic, D.; Sánchez-Vidaurre, S.; Waden, K.; Curin, M.; Grundström, J.; Gafvelin, G.; Cirkovic Velickovic, T.; Grönlund, H.; Thomas, W. R.; Valenta, R.; et al. The Cat Lipocalin Fel d 7 and Its Cross-Reactivity with the Dog Lipocalin Can f 1. Allergy: European Journal of Allergy and Clinical Immunology 2016, 71 (10), 1490–1495. https://doi.org/10.1111/all.12955. in Allergy
Wiley-Blackwell, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3651

Apostolović D, Sanchez-Vidaurre S, Waden K, Curin M, Grundström J, Gafvelin G, Ćirković-Veličković T, Gronlund H, Thomas WR, Valenta R, Hamsten C, van Hage M. Supplementary data for the article: Apostolovic, D.; Sánchez-Vidaurre, S.; Waden, K.; Curin, M.; Grundström, J.; Gafvelin, G.; Cirkovic Velickovic, T.; Grönlund, H.; Thomas, W. R.; Valenta, R.; et al. The Cat Lipocalin Fel d 7 and Its Cross-Reactivity with the Dog Lipocalin Can f 1. Allergy: European Journal of Allergy and Clinical Immunology 2016, 71 (10), 1490–1495. https://doi.org/10.1111/all.12955. in Allergy. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3651 .

Apostolović, Danijela, Sanchez-Vidaurre, Sara, Waden, Konrad, Curin, Mirela, Grundström, Jeanette, Gafvelin, Guro, Ćirković-Veličković, Tanja, Gronlund, Hans, Thomas, Wayne R., Valenta, Rudolf, Hamsten, Carl, van Hage, Marianne, "Supplementary data for the article: Apostolovic, D.; Sánchez-Vidaurre, S.; Waden, K.; Curin, M.; Grundström, J.; Gafvelin, G.; Cirkovic Velickovic, T.; Grönlund, H.; Thomas, W. R.; Valenta, R.; et al. The Cat Lipocalin Fel d 7 and Its Cross-Reactivity with the Dog Lipocalin Can f 1. Allergy: European Journal of Allergy and Clinical Immunology 2016, 71 (10), 1490–1495. https://doi.org/10.1111/all.12955" in Allergy (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3651 .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Sanchez-Vidaurre, Sara
AU  - Waden, Konrad
AU  - Curin, Mirela
AU  - Grundström, Jeanette
AU  - Gafvelin, Guro
AU  - Ćirković-Veličković, Tanja
AU  - Gronlund, Hans
AU  - Thomas, Wayne R.
AU  - Valenta, Rudolf
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2337
AB  - We investigated the prevalence of sensitization to the cat lipocalin Fel d 7 among 140 cat-sensitized Swedish patients and elucidated its allergenic activity and cross-reactivity with the dog lipocalin Can f 1. Sixty-five of 140 patients had IgE to rFel d 7 whereof 60 also had IgE to rCan f 1. A moderate correlation between IgE levels to rFel d 7 and rCan f 1 was found. rFel d 7 activated basophils in vitro and inhibited IgE binding to rCan f 1 in 4 of 13 patients, whereas rCan f 1 inhibited IgE binding to rFel d 7 in 7 of 13 patients. Fel d 7 and Can f 1 showed high similarities in protein structure and epitopes in common were found using cross-reactive antisera. Fel d 7 is a common allergen in a Swedish cat-sensitized population that cross-reacts with Can f 1, and may contribute to symptoms in cat-but also in dog-allergic patients.
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1
VL  - 71
IS  - 10
SP  - 1490
EP  - 1495
DO  - 10.1111/all.12955
ER  - 

@article{
author = "Apostolović, Danijela and Sanchez-Vidaurre, Sara and Waden, Konrad and Curin, Mirela and Grundström, Jeanette and Gafvelin, Guro and Ćirković-Veličković, Tanja and Gronlund, Hans and Thomas, Wayne R. and Valenta, Rudolf and Hamsten, Carl and van Hage, Marianne",
year = "2016",
abstract = "We investigated the prevalence of sensitization to the cat lipocalin Fel d 7 among 140 cat-sensitized Swedish patients and elucidated its allergenic activity and cross-reactivity with the dog lipocalin Can f 1. Sixty-five of 140 patients had IgE to rFel d 7 whereof 60 also had IgE to rCan f 1. A moderate correlation between IgE levels to rFel d 7 and rCan f 1 was found. rFel d 7 activated basophils in vitro and inhibited IgE binding to rCan f 1 in 4 of 13 patients, whereas rCan f 1 inhibited IgE binding to rFel d 7 in 7 of 13 patients. Fel d 7 and Can f 1 showed high similarities in protein structure and epitopes in common were found using cross-reactive antisera. Fel d 7 is a common allergen in a Swedish cat-sensitized population that cross-reacts with Can f 1, and may contribute to symptoms in cat-but also in dog-allergic patients.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1",
volume = "71",
number = "10",
pages = "1490-1495",
doi = "10.1111/all.12955"
}

Apostolović, D., Sanchez-Vidaurre, S., Waden, K., Curin, M., Grundström, J., Gafvelin, G., Ćirković-Veličković, T., Gronlund, H., Thomas, W. R., Valenta, R., Hamsten, C.,& van Hage, M.. (2016). The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. in Allergy
Wiley-Blackwell, Hoboken., 71(10), 1490-1495.
https://doi.org/10.1111/all.12955

Apostolović D, Sanchez-Vidaurre S, Waden K, Curin M, Grundström J, Gafvelin G, Ćirković-Veličković T, Gronlund H, Thomas WR, Valenta R, Hamsten C, van Hage M. The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1. in Allergy. 2016;71(10):1490-1495.
doi:10.1111/all.12955 .

Apostolović, Danijela, Sanchez-Vidaurre, Sara, Waden, Konrad, Curin, Mirela, Grundström, Jeanette, Gafvelin, Guro, Ćirković-Veličković, Tanja, Gronlund, Hans, Thomas, Wayne R., Valenta, Rudolf, Hamsten, Carl, van Hage, Marianne, "The cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1" in Allergy, 71, no. 10 (2016):1490-1495,
https://doi.org/10.1111/all.12955 . .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Tran, Thi Anh Thu
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - van Hage, Marianne
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1858
AB  - BackgroundRed meat allergy presents a novel form of food allergy with severe delayed allergic reactions where IgE antibodies are directed against the carbohydrate -Gal epitope. Food preparation and processing can influence the allergenicity of proteins. The aim of this study was to characterize the proteomic profile of different beef preparations and to investigate their -Gal reactivity and potential allergenicity. MethodsExtracts from raw, boiled, fried, and medium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles. IgE-binding proteins were identified using immunoblot-coupled proteomic analysis using sera from red meat-allergic patients. Presence of the -Gal epitope was verified using anti--Gal antibody and IgE inhibition immunoblot with -Gal. ResultsMultiple IgE-binding proteins were detected in the different beef preparations, many of which were also recognized by the anti--Gal antibody. Protein spots reacting with IgE in patient sera were analyzed by MS/MS, resulting in identification of 18 proteins with high identification scores. Seven of the 18 beef allergens identified using meat-allergic patient sera were also recognized by the anti--Gal monoclonal antibody, and four of them were stabile to thermal treatment. Furthermore, a dose-dependent inhibition of red meat-allergic patients' IgE to beef by -Gal was demonstrated. ConclusionsWe show that the -Gal epitope is commonly present in IgE-reactive beef proteins recognized by meat-allergic patients. Seven novel -Gal-containing IgE-binding proteins were identified, of which four were stable to heat treatment. Thus, the allergenicity of red meat proteins is preserved even upon different thermal cooking.
PB  - Wiley, Hoboken
T2  - Allergy
T1  - Immunoproteomics of processed beef proteins reveal novel galactose-alpha-1,3-galactose-containing allergens
VL  - 69
IS  - 10
SP  - 1308
EP  - 1315
DO  - 10.1111/all.12462
ER  - 

@article{
author = "Apostolović, Danijela and Tran, Thi Anh Thu and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and van Hage, Marianne",
year = "2014",
abstract = "BackgroundRed meat allergy presents a novel form of food allergy with severe delayed allergic reactions where IgE antibodies are directed against the carbohydrate -Gal epitope. Food preparation and processing can influence the allergenicity of proteins. The aim of this study was to characterize the proteomic profile of different beef preparations and to investigate their -Gal reactivity and potential allergenicity. MethodsExtracts from raw, boiled, fried, and medium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles. IgE-binding proteins were identified using immunoblot-coupled proteomic analysis using sera from red meat-allergic patients. Presence of the -Gal epitope was verified using anti--Gal antibody and IgE inhibition immunoblot with -Gal. ResultsMultiple IgE-binding proteins were detected in the different beef preparations, many of which were also recognized by the anti--Gal antibody. Protein spots reacting with IgE in patient sera were analyzed by MS/MS, resulting in identification of 18 proteins with high identification scores. Seven of the 18 beef allergens identified using meat-allergic patient sera were also recognized by the anti--Gal monoclonal antibody, and four of them were stabile to thermal treatment. Furthermore, a dose-dependent inhibition of red meat-allergic patients' IgE to beef by -Gal was demonstrated. ConclusionsWe show that the -Gal epitope is commonly present in IgE-reactive beef proteins recognized by meat-allergic patients. Seven novel -Gal-containing IgE-binding proteins were identified, of which four were stable to heat treatment. Thus, the allergenicity of red meat proteins is preserved even upon different thermal cooking.",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "Immunoproteomics of processed beef proteins reveal novel galactose-alpha-1,3-galactose-containing allergens",
volume = "69",
number = "10",
pages = "1308-1315",
doi = "10.1111/all.12462"
}

Apostolović, D., Tran, T. A. T., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& van Hage, M.. (2014). Immunoproteomics of processed beef proteins reveal novel galactose-alpha-1,3-galactose-containing allergens. in Allergy
Wiley, Hoboken., 69(10), 1308-1315.
https://doi.org/10.1111/all.12462

Apostolović D, Tran TAT, Hamsten C, Starkhammar M, Ćirković-Veličković T, van Hage M. Immunoproteomics of processed beef proteins reveal novel galactose-alpha-1,3-galactose-containing allergens. in Allergy. 2014;69(10):1308-1315.
doi:10.1111/all.12462 .

Apostolović, Danijela, Tran, Thi Anh Thu, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, van Hage, Marianne, "Immunoproteomics of processed beef proteins reveal novel galactose-alpha-1,3-galactose-containing allergens" in Allergy, 69, no. 10 (2014):1308-1315,
https://doi.org/10.1111/all.12462 . .

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 .