Abstract

Peanut allergy is one of the most severe food allergies due to its persistency and life-threatening character. Serum IgE from patients with documented peanut hypersensitivity reactions and synthetic peptides were used to screen the linear IgE-binding epitopes on the major peanut allergen, Ara h 1. Five major epitopes that bound peanut-specific serum IgE from more than 60% of patients tested were identified. Mutational analysis of the immunodominant epitope showed that single amino acid changes had dramatic effects on IgE-binding characteristics. Mapping and characterisation of the IgE-binding epitopes on Ara h1 could be used in future immunotherapeutic approaches for peanut allergy disease.

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