Effects of covalent conjugation with quercetin and its glycosides on the structure and allergenicity of Bra c p from bee pollen.

Enning Zhou, Xiaofeng Xue, Haoxie Xu, Liuwei Zhao, Liming Wu, Qiangqiang Li

Food chemistry 2023 Apr 16

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Profilin family members are potential pan-allergens in foods, presenting public health hazards. However, studies on the allergenicity modification of profilin allergens are limited. Herein, quercetin and its glycosides (isoquercitrin and rutin) were applied to modify the allergenicity of a profilin allergen (Bra c p) from Brassica campestris bee pollen. Results showed that only quercetin can be closely covalently bound to Bra c p among the three, and the binding site was located at the Cys98 residue. After covalently conjunction, the relative content of α-helix structure in Bra c p was reduced by 40.05%, while random coil was increased by 42.89%; moreover, the Tyr and Phe residues in Bra c p were masked. These structural changes could alter the conformational antigenic epitopes of Bra c p, resulting in its allergenicity reduction. Our findings might provide a technical foundation for reducing the allergenicity of bee pollen and foods containing profilin family allergens. Copyright © 2022 Elsevier Ltd. All rights reserved.

Citation

Enning Zhou, Xiaofeng Xue, Haoxie Xu, Liuwei Zhao, Liming Wu, Qiangqiang Li. Effects of covalent conjugation with quercetin and its glycosides on the structure and allergenicity of Bra c p from bee pollen. Food chemistry. 2023 Apr 16;406:135075