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Publication Date:
April 2009
ISSN:
1437-4315
DOI:
10.1515/BC.2009.063

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Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen

Petra Gruber1 / Gabriele Gadermaier1 / Roman Bauer1 / Richard Weiss1 / Stefan Wagner2 / Renaud Leonard3 / Heimo Breiteneder2 / Christof Ebner4 / Fatima Ferreira1 / Matthias Egger1

1Christian Doppler Laboratory for Allergy Diagnosis and Therapy, Department of Molecular Biology, University of Salzburg, Hellbrunnerstrasse 34, A-5020 Salzburg, Austria

2Department of Pathophysiology, Medical University of Vienna, Währinger Gürtel 18-20, A-1090 Vienna, Austria

3Department of Chemistry, University of Natural Resources and Applied Life Sciences, Muthgasse 18, A-1190 Vienna, Austria

4Allergy Clinic, Reumannplatz 17/1/4, A-1100 Vienna, Austria

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 5/6, Pages 445–451, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.063, April 2009

Publication History:
Received:
2009-01-19
Accepted:
2009-03-19
Published Online:
2009-04-10

Abstract

Artemisia vulgaris (mugwort) is one of the main causes of late summer pollinosis in Europe, with >95% of patients sensitized to the glycoallergen Art v 1. Despite the importance of this allergen, little is known about its cross-reactive behavior. Here we investigated the occurrence of conserved Art v 1 antigenic determinants in sources known to display clinically relevant cross-reactivity with mugwort pollen. For this purpose, monoclonal antibodies specific for a cysteine-stabilized epitope of the Art v 1 defensin domain and for carbohydrates attached to the proline domain were produced by hybridoma and phage display technologies. Using polyclonal Art v 1-specific rabbit sera and antibodies against both the Art v 1 carbohydrate and polypeptide moieties, we could identify cross-reactive structures in pollen from botanically related Asteraceae weeds (Artemisia absinthium, Helianthus annuus and Ambrosia sp.). Homologous allergens were also recognized by IgE from mugwort-sensitized patients and the reactivity could be decreased by serum pre-incubation with natural and recombinant Art v 1. As no cross-reactive structures could be found in foods associated with mugwort pollinosis, we conclude that Art v 1 is poorly involved in mugwort cross-reactivity to food allergens.

Keywords: ETH-2 phage library; glycoallergen; monoclonal antibody; mugwort pollen allergy; pDAP2/S vector; phage display

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