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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.
Biol Chem. 2009 May-Jun; 390(5-6):445-51.BC

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.

Authors+Show Affiliations

Christian Doppler Laboratory for Allergy Diagnosis and Therapy, Department of Molecular Biology, University of Salzburg, Hellbrunnerstrasse 34, A-5020 Salzburg, Austria.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19361284

Citation

Gruber, Petra, et al. "Role of the Polypeptide Backbone and Post-translational Modifications in Cross-reactivity of Art V 1, the Major Mugwort Pollen Allergen." Biological Chemistry, vol. 390, no. 5-6, 2009, pp. 445-51.
Gruber P, Gadermaier G, Bauer R, et al. Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen. Biol Chem. 2009;390(5-6):445-51.
Gruber, P., Gadermaier, G., Bauer, R., Weiss, R., Wagner, S., Leonard, R., Breiteneder, H., Ebner, C., Ferreira, F., & Egger, M. (2009). Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen. Biological Chemistry, 390(5-6), 445-51. https://doi.org/10.1515/BC.2009.063
Gruber P, et al. Role of the Polypeptide Backbone and Post-translational Modifications in Cross-reactivity of Art V 1, the Major Mugwort Pollen Allergen. Biol Chem. 2009;390(5-6):445-51. PubMed PMID: 19361284.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen. AU - Gruber,Petra, AU - Gadermaier,Gabriele, AU - Bauer,Roman, AU - Weiss,Richard, AU - Wagner,Stefan, AU - Leonard,Renaud, AU - Breiteneder,Heimo, AU - Ebner,Christof, AU - Ferreira,Fatima, AU - Egger,Matthias, PY - 2009/4/14/entrez PY - 2009/4/14/pubmed PY - 2009/7/17/medline SP - 445 EP - 51 JF - Biological chemistry JO - Biol. Chem. VL - 390 IS - 5-6 N2 - 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. SN - 1431-6730 UR - https://www.unboundmedicine.com/medline/citation/19361284/Role_of_the_polypeptide_backbone_and_post_translational_modifications_in_cross_reactivity_of_Art_v_1_the_major_mugwort_pollen_allergen_ L2 - https://www.degruyter.com/doi/10.1515/BC.2009.063 DB - PRIME DP - Unbound Medicine ER -