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  - CONF
AU  - Waden, Konrad
AU  - Apostolović, Danijela
AU  - Sanchez-Vidaurre, Sara
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  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2047
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - The novel cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1: structures, epitopes and allergenicity
VL  - 70
SP  - 517
EP  - 517
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2047
ER  - 

@conference{
author = "Waden, Konrad and Apostolović, Danijela and Sanchez-Vidaurre, Sara 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 = "2015",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "The novel cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1: structures, epitopes and allergenicity",
volume = "70",
pages = "517-517",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2047"
}

Waden, K., Apostolović, D., Sanchez-Vidaurre, S., Curin, M., Grundström, J., Gafvelin, G., Ćirković-Veličković, T., Gronlund, H., Thomas, W. R., Valenta, R., Hamsten, C.,& van Hage, M.. (2015). The novel cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1: structures, epitopes and allergenicity. in Allergy
Wiley-Blackwell, Hoboken., 70, 517-517.
https://hdl.handle.net/21.15107/rcub_cherry_2047

Waden K, Apostolović D, Sanchez-Vidaurre S, Curin M, Grundström J, Gafvelin G, Ćirković-Veličković T, Gronlund H, Thomas WR, Valenta R, Hamsten C, van Hage M. The novel cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1: structures, epitopes and allergenicity. in Allergy. 2015;70:517-517.
https://hdl.handle.net/21.15107/rcub_cherry_2047 .

Waden, Konrad, Apostolović, Danijela, Sanchez-Vidaurre, Sara, Curin, Mirela, Grundström, Jeanette, Gafvelin, Guro, Ćirković-Veličković, Tanja, Gronlund, Hans, Thomas, Wayne R., Valenta, Rudolf, Hamsten, Carl, van Hage, Marianne, "The novel cat lipocalin Fel d 7 and its cross-reactivity with the dog lipocalin Can f 1: structures, epitopes and allergenicity" in Allergy, 70 (2015):517-517,
https://hdl.handle.net/21.15107/rcub_cherry_2047 .

TY  - CONF
AU  - Waden, Konrad
AU  - Polović, Natalija
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/123456789/1409
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 dander-positive 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. © 2013 John Wiley & Sons A/S. Published by Blackwell Publishing Ltd.
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Dog saliva - an important source of dog allergens
VL  - 68
SP  - 35
EP  - 35
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1409
ER  - 

@conference{
author = "Waden, Konrad and Polović, Natalija 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 dander-positive 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. © 2013 John Wiley & Sons A/S. Published by Blackwell Publishing Ltd.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Dog saliva - an important source of dog allergens",
volume = "68",
pages = "35-35",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1409"
}

Waden, K., Polović, N., 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, 35-35.
https://hdl.handle.net/21.15107/rcub_cherry_1409

Waden K, Polović N, 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;68:35-35.
https://hdl.handle.net/21.15107/rcub_cherry_1409 .

Waden, Konrad, Polović, Natalija, 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 (2013):35-35,
https://hdl.handle.net/21.15107/rcub_cherry_1409 .

TY  - JOUR
AU  - van Hage, Marianne
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
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1488
PB  - Wiley-Blackwell, Hoboken
T2  - Allergy
T1  - Diversity of allergens contained in dog saliva REPLY
VL  - 68
IS  - 11
SP  - 1485
EP  - 1486
DO  - 10.1111/all.12264
ER  - 

@article{
author = "van Hage, Marianne and 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",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Diversity of allergens contained in dog saliva REPLY",
volume = "68",
number = "11",
pages = "1485-1486",
doi = "10.1111/all.12264"
}

van Hage, M., Polović, N., Waden, K., Binnmyr, J., Hamsten, C., Gronneberg, R., Palmberg, C., Milčić-Matić, N., Bergman, T.,& Gronlund, H.. (2013). Diversity of allergens contained in dog saliva REPLY. in Allergy
Wiley-Blackwell, Hoboken., 68(11), 1485-1486.
https://doi.org/10.1111/all.12264

van Hage M, Polović N, Waden K, Binnmyr J, Hamsten C, Gronneberg R, Palmberg C, Milčić-Matić N, Bergman T, Gronlund H. Diversity of allergens contained in dog saliva REPLY. in Allergy. 2013;68(11):1485-1486.
doi:10.1111/all.12264 .

van Hage, Marianne, Polović, Natalija, Waden, Konrad, Binnmyr, J., Hamsten, Carl, Gronneberg, R., Palmberg, C., Milčić-Matić, Natalija, Bergman, T., Gronlund, Hans, "Diversity of allergens contained in dog saliva REPLY" in Allergy, 68, no. 11 (2013):1485-1486,
https://doi.org/10.1111/all.12264 . .

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 .

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Atanasković-Marković, Marina
AU  - Ognjenović, Jana
AU  - Gronlund, Hans
AU  - van Hage, Marianne
AU  - Lantto, Raija
AU  - Sancho, Ana I.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1561
AB  - Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound
VL  - 56
IS  - 12
SP  - 1894
EP  - 1905
DO  - 10.1002/mnfr.201200179
ER  - 

@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Atanasković-Marković, Marina and Ognjenović, Jana and Gronlund, Hans and van Hage, Marianne and Lantto, Raija and Sancho, Ana I. and Ćirković-Veličković, Tanja",
year = "2012",
abstract = "Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound",
volume = "56",
number = "12",
pages = "1894-1905",
doi = "10.1002/mnfr.201200179"
}

Stanić-Vučinić, D., Stojadinović, M. M., Atanasković-Marković, M., Ognjenović, J., Gronlund, H., van Hage, M., Lantto, R., Sancho, A. I.,& Ćirković-Veličković, T.. (2012). Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 56(12), 1894-1905.
https://doi.org/10.1002/mnfr.201200179

Stanić-Vučinić D, Stojadinović MM, Atanasković-Marković M, Ognjenović J, Gronlund H, van Hage M, Lantto R, Sancho AI, Ćirković-Veličković T. Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. in Molecular Nutrition and Food Research. 2012;56(12):1894-1905.
doi:10.1002/mnfr.201200179 .

Stanić-Vučinić, Dragana, Stojadinović, Marija M., Atanasković-Marković, Marina, Ognjenović, Jana, Gronlund, Hans, van Hage, Marianne, Lantto, Raija, Sancho, Ana I., Ćirković-Veličković, Tanja, "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound" in Molecular Nutrition and Food Research, 56, no. 12 (2012):1894-1905,
https://doi.org/10.1002/mnfr.201200179 . .

TY  - CONF
AU  - Polović, Natalija
AU  - Bergman, T.
AU  - Milčić-Matić, Natalija
AU  - Gronlund, Hans
AU  - van Hage, Marianne
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1464
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Dog saliva - a source of dog allergens
VL  - 65
SP  - 105
EP  - 105
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1464
ER  - 

@conference{
author = "Polović, Natalija and Bergman, T. and Milčić-Matić, Natalija and Gronlund, Hans and van Hage, Marianne",
year = "2010",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Dog saliva - a source of dog allergens",
volume = "65",
pages = "105-105",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1464"
}

Polović, N., Bergman, T., Milčić-Matić, N., Gronlund, H.,& van Hage, M.. (2010). Dog saliva - a source of dog allergens. in Allergy
Wiley-Blackwell, Hoboken., 65, 105-105.
https://hdl.handle.net/21.15107/rcub_cherry_1464

Polović N, Bergman T, Milčić-Matić N, Gronlund H, van Hage M. Dog saliva - a source of dog allergens. in Allergy. 2010;65:105-105.
https://hdl.handle.net/21.15107/rcub_cherry_1464 .

Polović, Natalija, Bergman, T., Milčić-Matić, Natalija, Gronlund, Hans, van Hage, Marianne, "Dog saliva - a source of dog allergens" in Allergy, 65 (2010):105-105,
https://hdl.handle.net/21.15107/rcub_cherry_1464 .

TY  - JOUR
AU  - Osterlund, C.
AU  - Gronlund, Hans
AU  - Polović, Natalija
AU  - Sundstrom, S.
AU  - Gafvelin, Guro
AU  - Bucht, A.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/996
AB  - P gt Background House dust mites (HDM) are well-known as a source of indoor aeroallergens and for causing allergic airway diseases. Some proteolytic HDM allergens are known to activate respiratory epithelial cells to produce pro-inflammatory mediators, while there is limited knowledge regarding such activity among non-proteolytic HDM allergens. Objective To investigate whether Der p 2, a major non-proteolytic allergen of Dermatophagoides pteronyssinus, activates respiratory epithelial cells to produce mediators involved in asthma pathogenesis and to elucidate the mechanism of such activation. Methods The human bronchial epithelial cell line BEAS-2B, normal human bronchial epithelial (NHBE) cells and the alveolar epithelial cell line A549 were exposed to recombinant Der p 2. Following exposure, we analysed a panel of soluble mediators and cell adhesion receptors involved in asthma pathogenesis by promoting recruitment, survival and binding of inflammatory cells. The involvement of nuclear factor (NF)-kappa B and mitogen-activated protein kinases (MAPKs) was studied using specific inhibitors. Results Der p 2 activated bronchial BEAS-2B and NHBE cells, but not alveolar A549 cells. In BEAS-2B cells Der p 2 induced dose-dependent up-regulation in both mRNA level and protein secretion of granulocyte-macrophage colony-stimulating factor, IL-6, IL-8, monocyte-chemotactic protein-1 and macrophage inflammatory protein-3 alpha. Secretion as well as surface expression of intercellular adhesion molecule (ICAM)-1 was also up-regulated, which was associated with increased adhesion of monocytes to the epithelial cells. The release of cytokines and chemokines was regulated by NF-kappa B and MAPK activation in different ways, while expression of ICAM-1 was solely dependent on NF-kappa B activation. Conclusion These results show that Der p 2 activates respiratory epithelial cells, indicating that this non-proteolytic allergen, in addition to its immunogenic properties, can aggravate respiratory airway disease by adjuvant-like activation of the lung epithelium.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - The non-proteolytic house dust mite allergen Der p 2 induce NF-kappa B and MAPK dependent activation of bronchial epithelial cells
VL  - 39
IS  - 8
SP  - 1199
EP  - 1208
DO  - 10.1111/j.1365-2222.2009.03284.x
ER  - 

@article{
author = "Osterlund, C. and Gronlund, Hans and Polović, Natalija and Sundstrom, S. and Gafvelin, Guro and Bucht, A.",
year = "2009",
abstract = "P gt Background House dust mites (HDM) are well-known as a source of indoor aeroallergens and for causing allergic airway diseases. Some proteolytic HDM allergens are known to activate respiratory epithelial cells to produce pro-inflammatory mediators, while there is limited knowledge regarding such activity among non-proteolytic HDM allergens. Objective To investigate whether Der p 2, a major non-proteolytic allergen of Dermatophagoides pteronyssinus, activates respiratory epithelial cells to produce mediators involved in asthma pathogenesis and to elucidate the mechanism of such activation. Methods The human bronchial epithelial cell line BEAS-2B, normal human bronchial epithelial (NHBE) cells and the alveolar epithelial cell line A549 were exposed to recombinant Der p 2. Following exposure, we analysed a panel of soluble mediators and cell adhesion receptors involved in asthma pathogenesis by promoting recruitment, survival and binding of inflammatory cells. The involvement of nuclear factor (NF)-kappa B and mitogen-activated protein kinases (MAPKs) was studied using specific inhibitors. Results Der p 2 activated bronchial BEAS-2B and NHBE cells, but not alveolar A549 cells. In BEAS-2B cells Der p 2 induced dose-dependent up-regulation in both mRNA level and protein secretion of granulocyte-macrophage colony-stimulating factor, IL-6, IL-8, monocyte-chemotactic protein-1 and macrophage inflammatory protein-3 alpha. Secretion as well as surface expression of intercellular adhesion molecule (ICAM)-1 was also up-regulated, which was associated with increased adhesion of monocytes to the epithelial cells. The release of cytokines and chemokines was regulated by NF-kappa B and MAPK activation in different ways, while expression of ICAM-1 was solely dependent on NF-kappa B activation. Conclusion These results show that Der p 2 activates respiratory epithelial cells, indicating that this non-proteolytic allergen, in addition to its immunogenic properties, can aggravate respiratory airway disease by adjuvant-like activation of the lung epithelium.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "The non-proteolytic house dust mite allergen Der p 2 induce NF-kappa B and MAPK dependent activation of bronchial epithelial cells",
volume = "39",
number = "8",
pages = "1199-1208",
doi = "10.1111/j.1365-2222.2009.03284.x"
}

Osterlund, C., Gronlund, H., Polović, N., Sundstrom, S., Gafvelin, G.,& Bucht, A.. (2009). The non-proteolytic house dust mite allergen Der p 2 induce NF-kappa B and MAPK dependent activation of bronchial epithelial cells. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(8), 1199-1208.
https://doi.org/10.1111/j.1365-2222.2009.03284.x

Osterlund C, Gronlund H, Polović N, Sundstrom S, Gafvelin G, Bucht A. The non-proteolytic house dust mite allergen Der p 2 induce NF-kappa B and MAPK dependent activation of bronchial epithelial cells. in Clinical and Experimental Allergy. 2009;39(8):1199-1208.
doi:10.1111/j.1365-2222.2009.03284.x .

Osterlund, C., Gronlund, Hans, Polović, Natalija, Sundstrom, S., Gafvelin, Guro, Bucht, A., "The non-proteolytic house dust mite allergen Der p 2 induce NF-kappa B and MAPK dependent activation of bronchial epithelial cells" in Clinical and Experimental Allergy, 39, no. 8 (2009):1199-1208,
https://doi.org/10.1111/j.1365-2222.2009.03284.x . .

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Thunberg, Sarah
AU  - Polović, Natalija
AU  - Neimert-Andersson, Theresa
AU  - Gronlund, Hans
AU  - van Hage, Marianne
AU  - Gafvelin, Guro
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/934
AB  - Background: Endotoxins, comprised of bacterial cell wall lipopolysaccharides (LPS), have been reported to have both protective and exacerbating effects on the development and maintenance of allergic disease in humans and on markers of allergic inflammation in animal models of allergy. In this study, we investigated the effect of low concentrations of LPS on human peripheral blood mononuclear cells (PBMC) stimulated with the major cat allergen Fel d 1. Methods: Extensive purification of recombinant (r) Fel d 1 yielded essentially endotoxin-free rFel d 1 (0.2 ng LPS/mg protein). PBMCs prepared from 15 subjects having IgE to cat ( gt 0.7 kU(A)/l) and 8 subjects IgE negative to cat were stimulated with 2, 10 or 25 mu g/ml of rFel d 1 in the presence or absence of 50 pg/ml LPS. Proliferation was measured after 7 days of culture and supernatants were analyzed for IFN gamma, IL-5 and IL-10. Results: LPS (50 pg/ml) increased rFel d 1-stimulated proliferation of PBMCs both from subjects IgE-positive and subjects negative to cat allergens. PBMCs from 13 of the subjects did not proliferate in response to stimulation with 2 and 10 mu g/ml rFel d 1 alone but did so in the presence of LPS. Moreover, LPS increased the levels of rFel d 1-stimulated IFN gamma in cultures from cat-negative subjects, IL-5 from cat-positive subjects and IL-10 from both groups. Conclusion: Very low doses of LPS enhance proliferation and decrease the apparent threshold level for cell activation, prompting careful evaluation of allergen stimulated T cell activation in vitro. Copyright (C) 2007 S. Karger AG, Basel.
PB  - Karger, Basel
T2  - International Archives of Allergy and Immunology
T1  - Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells
VL  - 146
IS  - 1
SP  - 1
EP  - 10
DO  - 10.1159/000112497
ER  - 

@article{
author = "Ćirković-Veličković, Tanja and Thunberg, Sarah and Polović, Natalija and Neimert-Andersson, Theresa and Gronlund, Hans and van Hage, Marianne and Gafvelin, Guro",
year = "2008",
abstract = "Background: Endotoxins, comprised of bacterial cell wall lipopolysaccharides (LPS), have been reported to have both protective and exacerbating effects on the development and maintenance of allergic disease in humans and on markers of allergic inflammation in animal models of allergy. In this study, we investigated the effect of low concentrations of LPS on human peripheral blood mononuclear cells (PBMC) stimulated with the major cat allergen Fel d 1. Methods: Extensive purification of recombinant (r) Fel d 1 yielded essentially endotoxin-free rFel d 1 (0.2 ng LPS/mg protein). PBMCs prepared from 15 subjects having IgE to cat ( gt 0.7 kU(A)/l) and 8 subjects IgE negative to cat were stimulated with 2, 10 or 25 mu g/ml of rFel d 1 in the presence or absence of 50 pg/ml LPS. Proliferation was measured after 7 days of culture and supernatants were analyzed for IFN gamma, IL-5 and IL-10. Results: LPS (50 pg/ml) increased rFel d 1-stimulated proliferation of PBMCs both from subjects IgE-positive and subjects negative to cat allergens. PBMCs from 13 of the subjects did not proliferate in response to stimulation with 2 and 10 mu g/ml rFel d 1 alone but did so in the presence of LPS. Moreover, LPS increased the levels of rFel d 1-stimulated IFN gamma in cultures from cat-negative subjects, IL-5 from cat-positive subjects and IL-10 from both groups. Conclusion: Very low doses of LPS enhance proliferation and decrease the apparent threshold level for cell activation, prompting careful evaluation of allergen stimulated T cell activation in vitro. Copyright (C) 2007 S. Karger AG, Basel.",
publisher = "Karger, Basel",
journal = "International Archives of Allergy and Immunology",
title = "Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells",
volume = "146",
number = "1",
pages = "1-10",
doi = "10.1159/000112497"
}

Ćirković-Veličković, T., Thunberg, S., Polović, N., Neimert-Andersson, T., Gronlund, H., van Hage, M.,& Gafvelin, G.. (2008). Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells. in International Archives of Allergy and Immunology
Karger, Basel., 146(1), 1-10.
https://doi.org/10.1159/000112497

Ćirković-Veličković T, Thunberg S, Polović N, Neimert-Andersson T, Gronlund H, van Hage M, Gafvelin G. Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells. in International Archives of Allergy and Immunology. 2008;146(1):1-10.
doi:10.1159/000112497 .

Ćirković-Veličković, Tanja, Thunberg, Sarah, Polović, Natalija, Neimert-Andersson, Theresa, Gronlund, Hans, van Hage, Marianne, Gafvelin, Guro, "Low levels of endotoxin enhance allergen-stimulated proliferation and reduce the threshold for activation in human peripheral blood cells" in International Archives of Allergy and Immunology, 146, no. 1 (2008):1-10,
https://doi.org/10.1159/000112497 . .

TY  - JOUR
AU  - Kaiser, Liselotte
AU  - Ćirković-Veličković, Tanja
AU  - Badia-Martinez, Daniel
AU  - Adedoyin, Justus
AU  - Thunberg, Sarah
AU  - Hallen, Dan
AU  - Berndt, Kurt
AU  - Gronlund, Hans
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Achour, Adnane
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/848
AB  - Felis domesticus allergen 1(Fel d 1) is a 35 kDa tetrameric glycoprotein formed by two heterodimers which elicits IgE responses in 95% of patients with allergy to cat. We have previously established in vitro conditions for the appropriate folding of recombinant Fel d 1 using a direct linkage of chain I to chain 2 (construct Fel d 1 (1 + 2)) and chain 2 to chain 1 (construct Fel d 1 (2 + 1)). Although the crystal structure of Fel d 1 (2 + 1) revealed a striking structural similarity to that of uteroglobin, a steroid-inducible cytokine-like molecule with anti-inflammatory and immunomodulatory properties, no functional tetrameric form of Fel d I could be identified. Here we present the crystal structure of the Fel d I (1 +2) tetramer at 1.6 angstrom resolution. Interestingly, the crystal structure of tetrameric Fel d I reveals two different calcium-binding sites. Symmetrically positioned on each side of the Fel d 1 tetramer, the external Ca2+ -binding sites correspond to a putative Ca2+- binding site previously suggested for uteroglobin. The second Ca2+-binding site lies within the dimerization interface, stabilizing the formation of the Fel d 1 tetramer, and inducing important local conformational changes that directly govern the shape of two water-filled cavities. The crystal structure suggests a potential portal for an unknown ligand. Alternatively, the two cavities could be used by the allergen as a conditional inner space allowing for the spatial rearrangement of centrally localized side-chains, such as Asp130, without altering the overall fold of the molecule. The striking structural similarity of the major cat allergen to uteroglobin, coupled to the identification in the present study of a common Ca2+ -binding site, let us speculate that Fel d I could provoke an allergic response through the modulation of phospholipase A2, by sequestering Ca ions in a similar manner as previously suggested for uteroglobin. (c) 2007 Elsevier Ltd. All rights reserved.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Molecular Biology
T1  - Structural characterization of the tetrameric form of the major cat allergen Fel d 1
VL  - 370
IS  - 4
SP  - 714
EP  - 727
DO  - 10.1016/j.jmb.2007.04.074
ER  - 

@article{
author = "Kaiser, Liselotte and Ćirković-Veličković, Tanja and Badia-Martinez, Daniel and Adedoyin, Justus and Thunberg, Sarah and Hallen, Dan and Berndt, Kurt and Gronlund, Hans and Gafvelin, Guro and van Hage, Marianne and Achour, Adnane",
year = "2007",
abstract = "Felis domesticus allergen 1(Fel d 1) is a 35 kDa tetrameric glycoprotein formed by two heterodimers which elicits IgE responses in 95% of patients with allergy to cat. We have previously established in vitro conditions for the appropriate folding of recombinant Fel d 1 using a direct linkage of chain I to chain 2 (construct Fel d 1 (1 + 2)) and chain 2 to chain 1 (construct Fel d 1 (2 + 1)). Although the crystal structure of Fel d 1 (2 + 1) revealed a striking structural similarity to that of uteroglobin, a steroid-inducible cytokine-like molecule with anti-inflammatory and immunomodulatory properties, no functional tetrameric form of Fel d I could be identified. Here we present the crystal structure of the Fel d I (1 +2) tetramer at 1.6 angstrom resolution. Interestingly, the crystal structure of tetrameric Fel d I reveals two different calcium-binding sites. Symmetrically positioned on each side of the Fel d 1 tetramer, the external Ca2+ -binding sites correspond to a putative Ca2+- binding site previously suggested for uteroglobin. The second Ca2+-binding site lies within the dimerization interface, stabilizing the formation of the Fel d 1 tetramer, and inducing important local conformational changes that directly govern the shape of two water-filled cavities. The crystal structure suggests a potential portal for an unknown ligand. Alternatively, the two cavities could be used by the allergen as a conditional inner space allowing for the spatial rearrangement of centrally localized side-chains, such as Asp130, without altering the overall fold of the molecule. The striking structural similarity of the major cat allergen to uteroglobin, coupled to the identification in the present study of a common Ca2+ -binding site, let us speculate that Fel d I could provoke an allergic response through the modulation of phospholipase A2, by sequestering Ca ions in a similar manner as previously suggested for uteroglobin. (c) 2007 Elsevier Ltd. All rights reserved.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Molecular Biology",
title = "Structural characterization of the tetrameric form of the major cat allergen Fel d 1",
volume = "370",
number = "4",
pages = "714-727",
doi = "10.1016/j.jmb.2007.04.074"
}

Kaiser, L., Ćirković-Veličković, T., Badia-Martinez, D., Adedoyin, J., Thunberg, S., Hallen, D., Berndt, K., Gronlund, H., Gafvelin, G., van Hage, M.,& Achour, A.. (2007). Structural characterization of the tetrameric form of the major cat allergen Fel d 1. in Journal of Molecular Biology
Academic Press Ltd- Elsevier Science Ltd, London., 370(4), 714-727.
https://doi.org/10.1016/j.jmb.2007.04.074

Kaiser L, Ćirković-Veličković T, Badia-Martinez D, Adedoyin J, Thunberg S, Hallen D, Berndt K, Gronlund H, Gafvelin G, van Hage M, Achour A. Structural characterization of the tetrameric form of the major cat allergen Fel d 1. in Journal of Molecular Biology. 2007;370(4):714-727.
doi:10.1016/j.jmb.2007.04.074 .

Kaiser, Liselotte, Ćirković-Veličković, Tanja, Badia-Martinez, Daniel, Adedoyin, Justus, Thunberg, Sarah, Hallen, Dan, Berndt, Kurt, Gronlund, Hans, Gafvelin, Guro, van Hage, Marianne, Achour, Adnane, "Structural characterization of the tetrameric form of the major cat allergen Fel d 1" in Journal of Molecular Biology, 370, no. 4 (2007):714-727,
https://doi.org/10.1016/j.jmb.2007.04.074 . .