Skip to content
Licensed Unlicensed Requires Authentication Published by De Gruyter April 10, 2009

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

  • Petra Gruber , Gabriele Gadermaier , Roman Bauer , Richard Weiss , Stefan Wagner , Renaud Leonard , Heimo Breiteneder , Christof Ebner , Fatima Ferreira and Matthias Egger
From the journal Biological Chemistry

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.


Corresponding author

Received: 2009-01-19
Accepted: 2009-05-19
Published Online: 2009-04-10
Published in Print: 2009-05-28

©2009 by Walter de Gruyter Berlin New York

Downloaded on 25.4.2024 from https://www.degruyter.com/document/doi/10.1515/BC.2009.063/html
Scroll to top button