Conserved digestion-resistant peptides contribute to wheat cross-reactivity with other cereals

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Wheat is a major food allergen, and digestion-resistant peptides play a critical role in allergic responses and cross-reactivity. In this study, an in vitro simulated digestion model combined with mass spectrometry was used to examine the conservation of digestion-resistant allergenic sequences among cereals grains. Results showed that wheat, barley, and rye share several core digestion-resistant allergenic peptides, including “PLVQQQ” and “QPFPQ”. These peptides showed more than 50% sequence identity to known wheat gliadin allergenic sequences. Notably, “IIPQQPQQPFL” from wheat ω-gliadin and “VRVPVPQL” from rye α-secalin remained stable after 60 min of intestinal digestion. In contrast, oat-derived peptides showed very low homology to reported wheat allergenic sequences. ELISA using sera from 24 patients with wheat allergy revealed significant IgG/IgE cross-reactivity among wheat, barley, and rye, but no significant cross-reactivity with oat. KU812 cell assays further showed that all three grains induced mediator release. These findings indicate that conserved digestion-resistant allergenic sequences are key contributors to cross-reactivity among wheat, barley, and rye. This study provides a scientific basis for the dietary management of cereal allergy and the development of low-allergenicity cereal-based foods.