Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides

Alexander C.Y. Foo, Jacqueline B. Nesbit, Stephen A.Y. Gipson, Hsiaopo Cheng, Pierre Bushel, Eugene F. DeRose, Catherine H. Schein, Suzanne S. Teuber, Barry K. Hurlburt, Soheila J. Maleki, Geoffrey A. Mueller

Research output: Contribution to journalArticlepeer-review


Vicilin-buried peptides (VBPs) from edible plants are derived from the N-terminal leader sequences (LSs) of seed storage proteins. VBPs are defined by a common α-hairpin fold mediated by conserved CxxxCx(10-14)CxxxC motifs. Here, peanut and walnut VBPs were characterized as potential mediators of both peanut/walnut allergenicity and cross-reactivity despite their low (∼17%) sequence identity. The structures of one peanut (AH1.1) and 3 walnut (JR2.1, JR2.2, JR2.3) VBPs were solved using solution NMR, revealing similar α-hairpin structures stabilized by disulfide bonds with high levels of surface similarity. Peptide microarrays identified several peptide sequences primarily on AH1.1 and JR2.1, which were recognized by peanut-, walnut-, and dual-allergic patient IgE, establishing these peanut and walnut VBPs as potential mediators of allergenicity and cross-reactivity. JR2.2 and JR2.3 displayed extreme resilience against endosomal digestion, potentially hindering epitope generation and likely contributing to their reduced allergic potential.

Original languageEnglish (US)
Pages (from-to)2389-2400
Number of pages12
JournalJournal of Agricultural and Food Chemistry
Issue number7
StatePublished - Feb 23 2022


  • cross-reactivity
  • IgE epitopes
  • vicilin-buried peptide
  • α-hairpinin

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)


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