TY - JOUR
T1 - Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides
AU - Foo, Alexander C.Y.
AU - Nesbit, Jacqueline B.
AU - Gipson, Stephen A.Y.
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.
N1 - Publisher Copyright:
© 2022 American Chemical Society
PY - 2022/2/23
Y1 - 2022/2/23
N2 - 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.
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.
KW - IgE epitopes
KW - cross-reactivity
KW - vicilin-buried peptide
KW - α-hairpinin
UR - https://www.scopus.com/pages/publications/85124911798
UR - https://www.scopus.com/pages/publications/85124911798#tab=citedBy
U2 - 10.1021/acs.jafc.1c07225
DO - 10.1021/acs.jafc.1c07225
M3 - Article
C2 - 35139305
AN - SCOPUS:85124911798
SN - 0021-8561
VL - 70
SP - 2389
EP - 2400
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 7
ER -