| Literature DB >> 35139305 |
Alexander C Y Foo1, Jacqueline B Nesbit2, Stephen A Y Gipson2, Hsiaopo Cheng2, Pierre Bushel1, Eugene F DeRose1, Catherine H Schein3, Suzanne S Teuber4, Barry K Hurlburt2, Soheila J Maleki2, Geoffrey A Mueller1.
Abstract
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.Entities:
Keywords: IgE epitopes; cross-reactivity; vicilin-buried peptide; α-hairpinin
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Year: 2022 PMID： 35139305 PMCID： PMC8959100 DOI： 10.1021/acs.jafc.1c07225
Source DB: PubMed Journal: J Agric Food Chem ISSN： 0021-8561 Impact factor: 5.279