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  - CONF
AU  - Tran, Thi Anh Thu
AU  - Grundström, Jeanette
AU  - Krstić-Ristivojević, Maja
AU  - Vukojević, Vladana
AU  - Apostolović, Danijela
AU  - Hamsten, Carl
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2309
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - In vitro uptake of alpha-Gal containing protein by human monocyte derived dendritic cells
VL  - 71
SP  - 284
EP  - 284
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2309
ER  - 

@conference{
author = "Tran, Thi Anh Thu and Grundström, Jeanette and Krstić-Ristivojević, Maja and Vukojević, Vladana and Apostolović, Danijela and Hamsten, Carl and Gafvelin, Guro and van Hage, Marianne",
year = "2016",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "In vitro uptake of alpha-Gal containing protein by human monocyte derived dendritic cells",
volume = "71",
pages = "284-284",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2309"
}

Tran, T. A. T., Grundström, J., Krstić-Ristivojević, M., Vukojević, V., Apostolović, D., Hamsten, C., Gafvelin, G.,& van Hage, M.. (2016). In vitro uptake of alpha-Gal containing protein by human monocyte derived dendritic cells. in Allergy
Wiley-Blackwell, Hoboken., 71, 284-284.
https://hdl.handle.net/21.15107/rcub_cherry_2309

Tran TAT, Grundström J, Krstić-Ristivojević M, Vukojević V, Apostolović D, Hamsten C, Gafvelin G, van Hage M. In vitro uptake of alpha-Gal containing protein by human monocyte derived dendritic cells. in Allergy. 2016;71:284-284.
https://hdl.handle.net/21.15107/rcub_cherry_2309 .

Tran, Thi Anh Thu, Grundström, Jeanette, Krstić-Ristivojević, Maja, Vukojević, Vladana, Apostolović, Danijela, Hamsten, Carl, Gafvelin, Guro, van Hage, Marianne, "In vitro uptake of alpha-Gal containing protein by human monocyte derived dendritic cells" in Allergy, 71 (2016):284-284,
https://hdl.handle.net/21.15107/rcub_cherry_2309 .

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  - JOUR
AU  - Perovic, I.
AU  - Milovanovic, M.
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/600
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
VL  - 39
IS  - 3
SP  - 435
EP  - 446
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perovic, I. and Milovanovic, M. and Stanić, Dragana and Burazer, Lidija M. and Petrović, D. and Milčić-Matić, Natalija and Gafvelin, Guro and van Hage, Marianne and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
volume = "39",
number = "3",
pages = "435-446",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perovic, I., Milovanovic, M., Stanić, D., Burazer, L. M., Petrović, D., Milčić-Matić, N., Gafvelin, G., van Hage, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perovic I, Milovanovic M, Stanić D, Burazer LM, Petrović D, Milčić-Matić N, Gafvelin G, van Hage M, Jankov RM, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perovic, I., Milovanovic, M., Stanić, Dragana, Burazer, Lidija M., Petrović, D., Milčić-Matić, Natalija, Gafvelin, Guro, van Hage, Marianne, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

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 . .