EPITOPE SPECIFICITY OF THE MAJOR PEANUT ALLERGEN, ARA-H-II

The antigenic and allergenic structure of Ara h II, a major allergen o f peanuts, was investigated with the use of four monoclonal antibodies obtained from BALB/c mice immunized with purified Ara h II. Our previ ous studies with monoclonal antibodies generated to peanut allergens s howed this method to be useful for epitope mapping. When used as a sol id phase in an ELISA, these monoclonal antibodies captured peanut anti gen, which bound human IgE from patients with positive peanut challeng e responses. The Ara h II monoclonal antibodies were found to be speci fic for peanut antigens when binding for other legumes was examined. I n ELISA inhibition studies with the monoclonal antibodies, we identifi ed two different antigenic sites on Ara h II. In similar studies with pooled human IgE serum from patients with positive challenge responses to peanuts, we identified two closely related IgE-binding epitopes. T hese characterized monoclonal antibodies to Ara h II will be useful fo r future studies to immunoaffinity purify the Ara h II allergen and to use in conjunction with recombinant technology for determining struct ure-function relationships.