Tertiary structure of peanut allergen ara h 1

摘要

Ara h 1, a major peanut allergen, has been isolated and shown to contain 23 linear IgE-binding epitopes, 6-10 residues in length. Analysis of wild-type and mutant peptides with single amino acids substitutions showed that amino acids residing in the middle of the epitope were more critical for IgE binding; that polar charged residues occurred more frequently within the epitope while apolar residues were more important for IgE binding; and that a single amino acid substitution in an epitope resulted in a loss of ability to bind IgE. In addition, a homology-based molecular model of the Ara h 1 protein representing residues 171-586 was made and allowed visualization of epitopes 10-22. The majority of these epitopes appear clustered and many of the critical amino acids involved in binding are evenly distributed on the surface. The information from the mutational analysis and the molecular model will aid in the design of immunotherapies.