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

doi:10.1021/acs.jafc.1c07225

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

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

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.

Original language	English (US)
Pages (from-to)	2389-2400
Number of pages	12
Journal	Journal of Agricultural and Food Chemistry
Volume	70
Issue number	7
DOIs	https://doi.org/10.1021/acs.jafc.1c07225
State	Published - Feb 23 2022

Keywords

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

ASJC Scopus subject areas

General Chemistry
General Agricultural and Biological Sciences

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10.1021/acs.jafc.1c07225

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Foo, A. C. Y., Nesbit, J. B., Gipson, S. A. Y., Cheng, H., Bushel, P., DeRose, E. F., Schein, C. H., Teuber, S. S., Hurlburt, B. K., Maleki, S. J., & Mueller, G. A. (2022). Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides. Journal of Agricultural and Food Chemistry, 70(7), 2389-2400. https://doi.org/10.1021/acs.jafc.1c07225

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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.",

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AU - Nesbit, Jacqueline B.

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AU - Cheng, Hsiaopo

AU - Bushel, Pierre

AU - DeRose, Eugene F.

AU - Schein, Catherine H.

AU - Teuber, Suzanne S.

AU - Hurlburt, Barry K.

AU - Maleki, Soheila J.

AU - Mueller, Geoffrey A.

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

Abstract

Keywords

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