A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patients

• Published in: Molecular immunology 2006-02, Vol.43 (3), p.268-278
• Main Authors: Mittag, Diana, Batori, Vincent, Neudecker, Philipp, Wiche, Regina, Friis, Esben P., Ballmer-Weber, Barbara K., Vieths, Stefan, Roggen, Erwin L.
• Format: Article
• Language: English
• Subjects: 2S Albumins, Plant; Adolescent; Adult; Allergens - blood; Allergens - immunology; Antibody Specificity - immunology; Antigens, Plant; Bet v 1; Cross Reactions; Cross-reactivity; Enzyme-Linked Immunosorbent Assay; Epitope Mapping; Epitopes - immunology; Female; Food Hypersensitivity - blood; Food Hypersensitivity - immunology; Humans; IgE epitope; Immunoglobulin E - analysis; Immunoglobulin E - blood; Immunoglobulin E - immunology; Male; Peptide Library; Peptide mimic; Phage-display; Plant Proteins - blood; Plant Proteins - immunology; Soybean Proteins - immunology; Structural Homology, Protein
• ISSN: 0161-5890; 1872-9142
• DOI: 10.1016/j.molimm.2005.02.008

A clinically relevant allergic reaction requires recognition of at least two different epitopes on the surface of the allergen by IgE. These epitopes may be specific or cross-reactive. Moreover, patterns of IgE reactivity may be patient-specific. The aim of our study was to compare specific and cross-reactive IgE epitopes and epitope patterns between individual patients. We used Bet v 1-related food allergy as a model. Five patients were investigated by cross-competitive ELISA for specific and cross-reacting IgE to Bet v 1, and its homologues Gly m 4 (soybean), Ara h 8 (peanut), and Pru av 1 (cherry). Allergen-specific as well as cross-reactive IgE epitopes were assessed by competitive immunoscreening of a phage-displayed random 7-mer peptide library using polyclonal purified IgE from individual sera. The resulting peptide mimics were mapped on the surface of the 3D-structure of the allergens using a computer-based algorithm. Competitive immunoscreening and epitope mapping identified patient-specific IgE epitope patterns. However, one IgE-binding surface area that was recognized by all patients and two recognized by three patients were identified on all four proteins. These results are consistent with the determination of IgE cross-reactivity of the individual patients’ sera against the four recombinant allergens by cross-competitive ELISA. Selection of phage-displayed peptide mimics with serum IgE from allergic patients in combination with computer-based mapping of the peptide mimics onto the surface of the three-dimensional allergen structure is a promising novel tool to investigate IgE epitope specificity in individual patients. Such basic information on epitope structure may be used for prediction of cross-reactivity and potential allergenicity of novel foods.