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 - Funding Information:
This research was supported in part by the Intramural Research Program of the National Institute of Environmental Health Sciences (Z01-ES102906, G.A.M.) and the National Institute of Allergy and Infectious Disease (NIAID-R21 AI135397 and 1R01AI165866, C.H.S.) and also funded by the US Department of Agriculture: Agricultural Research Service (ARS-6054-43440-044-00D) and the National Institute for Food and Agriculture/National Peanut Board (NIFA-60-6054-7-003 SJM/BKH/JBN). The structures for AH1.1, JR2.1, JR2.2, and JR2.3 were submitted to the Protein Data Bank and the Biological Magnetic Resonance Bank under the access codes PBD ID 7LXK BMRB 30875, PDB ID 7LVF BRMB ID 30870, PDB ID 7LVG BMRB 30871, and PDB ID 7LVE BRMB ID 30869, respectively.
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 - cross-reactivity
KW - IgE epitopes
KW - vicilin-buried peptide
KW - α-hairpinin
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U2 - 10.1021/acs.jafc.1c07225
DO - 10.1021/acs.jafc.1c07225
M3 - Article
C2 - 35139305
AN - SCOPUS:85124911798
VL - 70
SP - 2389
EP - 2400
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 7
ER -