Identification of a New IgE-Binding Epitope of Peanut Oleosin That Cross-Reacts with Buckwheat

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  • KOBAYASHI Shoko
    Research Center for Food Safety, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • KATSUYAMA Shinta
    Research Center for Food Safety, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • WAGATSUMA Tamae
    Department of Food and Life Science, Takasaki University of Health and Welfare
  • OKADA Shinji
    Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • TANABE Soichi
    Graduate School of Biosphere Science, Hiroshima University

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Abstract

Peanut and buckwheat induce a severe allergic reaction, anaphylaxis, which is considered to be mediated by immunoglobulin E (IgE). We identified in this study a new IgE-binding epitope of the peanut allergen that cross-reacted with buckwheat. The phosphate-buffered saline-soluble fraction of buckwheat inhibited the binding between IgE and the peanut allergen. A cross-reactive peptide was isolated from the α-chymotrypsin hydrolysate of peanut. Based on the amino acid sequence and mass spectrometric analysis data, the peptide was identified as Ser-Asp-Gln-Thr-Arg-Thr-Gly-Tyr (SDQTRTGY); this sequence is identical to amino acids 2–9 in the N-terminal hydrophilic domain of oleosin 3 which is located on the surface of the lipid storage body. Synthetic SDQTRTGY was found to bind with IgE in the sera of all eight peanut-allergic patients tested. Since many foods of plant origin contain oleosin, the possibility of an anaphylactic cross-reaction in allergic patients should always be considered.

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