Covalent conjugation with quercetin mitigates allergenicity of the bee pollen allergen Bra c p in a murine model.

Abstract

Profilin family members are highly conserved food allergens that can cause widespread cross-allergic reactions. Our previous research has demonstrated that the covalent conjunction with quercetin can disrupt the conformational epitopes of a profilin allergen, Bra c p. In this study, we further investigated the intrinsic molecular mechanisms using molecular dynamics simulations. Moreover, the allergenic potential of Bra c p and its conjugate with quercetin was assessed in BALB/c mice. The results showed that continuous interaction with quercetin increased the molecular motion of Bra c p, causing changes to its α-helices and exposing hydrophobic residues which altered antigenic epitopes. Additionally, mice treated with Bra c p-quercetin conjugate showed reduced allergic reactions compared to those treated with Bra c p alone by regulating purine metabolism, calcium signaling, and CD4CD25Tregs proportion. Quercetin conjugation decreases the allergenicity of Bra c p, providing a scientific foundation for reducing the profilin allergens in food.