Biochemical and structural analysis of the IgE binding sites on Ara h1, an abundant and highly allergenic peanut protein

David S. Shin, Cesar M. Compadre, Soheila J. Maleki, Randall A. Kopper, Hugh Sampson, Shau K. Huang, A. Wesley Burks, Gary A. Bannon

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226 引文 斯高帕斯(Scopus)

摘要

Allergy to peanut is a significant IgE-mediated health problem because of the high prevalence, potential severity, and chronicity of the reaction. Ara h1, an abundant peanut protein, is recognized by serum IgE from >90% of peanut-sensitive individuals. It has been shown to belong to the vicilin family of seed storage proteins and to contain 23 linear IgE binding epitopes. In this communication, we have determined the critical amino acids within each of the IgE binding epitopes of Arahi that are important for immunoglobulin binding. Surprisingly, substitution of a single amino acid within each of the epitopes led to loss of IgE binding. In addition, hydrophobic residues appeared to be most critical for IgE binding. The position of each of the IgE binding on a homology-based molecular model of Ara hi showed that they were clustered into two main regions, despite their more even distribution in the primary sequence. Finally, we have shown that Ara hi forms a stable trimer by the use of a reproducible fluorescence assay. This information will be important in studies designed to reduce the risk of peanut-induced anaphylaxis by lowering the IgE binding capacity of the allergen.

原文英語
頁(從 - 到)13753-13759
頁數7
期刊Journal of Biological Chemistry
273
發行號22
DOIs
出版狀態已發佈 - 5月 29 1998
對外發佈

ASJC Scopus subject areas

  • 生物化學
  • 分子生物學
  • 細胞生物學

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