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.

Profilin 家族成员是食品中潜在的泛过敏原，对公众健康构成危害。然而，关于profilin变应原的变应原性修饰的研究是有限的。在此，应用槲皮素及其糖苷（异槲皮苷和芦丁）来改变来自油菜的 profilin 过敏原 (Bra cp) 的过敏性蜂花粉。结果表明，三者中只有槲皮素能与Bra cp紧密共价结合，结合位点位于Cys98残基。共价连接后，Bra cp中α-螺旋结构的相对含量减少了40.05%，无规卷曲增加了42.89%；此外，Bra cp 中的 Tyr 和 Phe 残基被掩盖了。这些结构变化可能会改变 Bra cp 的构象抗原表位，从而降低其过敏性。我们的研究结果可能为降低蜂花粉和含有 profilin 家族过敏原的食物的过敏性提供技术基础。