Epitopes described in "Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen."

Article Authors:Regina Wiche; Michaela Gubesch; Herbert König; Kay Fötisch; Andreas Hoffmann; Andrea Wangorsch; Stephan Scheurer; Stefan Vieths
Article Title:Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen.
Reference Detail
Reference ID:1012603
Abstract:Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) Pru av 1 has already been identified. This is the so-called 'P-loop' region, which encompasses amino acid residues around position 45 and is found on the two virtually identical tertiary protein structures. We tried to determine an additional IgE cross-reacting patch on Pru av 1 and Bet v 1. The putative IgE-binding region on Pru av 1 was localized with a mAb (monoclonal antibody) that was generated against Bet v 1, and cross-reacts with several Bet v 1 homologues in food and inhibits the binding of patients' IgE to Pru av 1. mAb reactivity pattern was analysed and amino acid positions 28 and 108 of Pru av 1 were selected and mutated by site-directed mutagenesis. The Pru av 1 mutants were produced as recombinant proteins and characterized for their folding, mAb- and IgE-binding capacity and allergenic potency with a cellular assay using the humanized rat basophilic leukaemia cell line RBL-25/30. Amino acid position 28 is involved in a second major IgE-binding region on Pru av 1 and probably on Bet v 1. The identification of this second major IgE-binding region is an essential prerequisite to understand the phenomenon of cross-reactivity and its clinical consequences, and to produce hypoallergenic proteins for an improved immunotherapy of type I allergy.
Affiliations:Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51-59, 63225 Langen, Germany.
Reference Type:Literature
PubMed ID:15330760
Journal:Biochem J
Journal Volume:385
Article Pages:319-27
Journal ISSN:0264-6021
Article Chemical List:Allergens;Antibodies, Monoclonal;Antigens, Plant;Epitopes;Pru av 1 allergen, Prunus avium;Immunoglobulin E
Article MeSH List:Allergens(chemistry; genetics; immunology); Amino Acid Sequence; Antibodies, Monoclonal(immunology); Antibody Specificity; Antigens, Plant; Circular Dichroism; Cross Reactions(immunology); Epitopes(chemistry; genetics; immunology); Food Hypersensitivity(immunology); Humans; Immunoglobulin E(immunology); Models, Molecular; Molecular Sequence Data; Mutation(genetics); Pollen(immunology); Protein Structure, Secondary; Prunus(chemistry; genetics; immunology); Surface Plasmon Resonance
Curation Last Updated:2015-06-05 01:21:35