Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides
journal contributionposted on 09.02.2022, 23:13 authored by 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
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.
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terminal leader sequencesseed storage proteinshairpin fold mediatedrevealing similar αreduced allergic potentialallergic patient igehairpin structures stabilizedburied peptides vicilinreactivity among walnutburied peptidespotential mediatorscommon αpeanut vicilinsurface similarityreactivity despitelikely contributingige crosshigh levelsendosomal digestionedible plantsdisulfide bondscxxxc motifsconserved cxxxcx