7LXK

Ara h 1 leader sequence, Ara h 1.0101 (25-83) A25G

Summary for 7LXK

• Entry DOI: 10.2210/pdb7lxk/pdb
• NMR Information: BMRB: 30875
• Descriptor: Allergen Ara h 1, clone P41B (1 entity in total)
• Functional Keywords: peanut allergen, allergen
• Biological source: Arachis hypogaea (Peanut)
• Total number of polymer chains: 1
• Total formula weight: 6733.50

Authors

Mueller, G.,London, R. (deposition date: 2021-03-03, release date: 2022-03-09, Last modification date: 2024-10-23)

Primary citation

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.
Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides.
J.Agric.Food Chem., 70:2389-2400, 2022

PubMed 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 CxxxCxCxxxC 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.

PubMed: 35139305
DOI: 10.1021/acs.jafc.1c07225

Experimental method

SOLUTION NMR