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

被引：5

作者：

Zhou, Enning ^{[1
]}

Li, Qiangqiang ^{[1
]}

Xu, Rui ^{[2
]}

Pan, Fei ^{[1
]}

Tao, Yuxiao ^{[1
]}

Li, Xiangxin ^{[1
]}

Xue, Xiaofeng ^{[1
]}

Wu, Liming ^{[1
]}

机构：

[1] Chinese Acad Agr Sci CAAS, Inst Apicultural Res, State Key Lab Resource Insects, Beijing 100093, Peoples R China

[2] Chinese Acad Agr Sci CAAS, Inst Food Sci & Technol, Beijing 100193, Peoples R China

来源：

FOOD CHEMISTRY | 2024年 / 436卷

基金：

中国国家自然科学基金;

关键词：

Bra c p; Quercetin; Covalent conjunction; Allergenicity; Purine metabolism; Calcium signaling; RYANODINE RECEPTOR; INFLAMMATION; ADENOSINE; PROFILIN;

D O I：

10.1016/j.foodchem.2023.137722

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

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 alpha-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 CD4+CD25+ Tregs proportion. Quercetin conjugation decreases the allergenicity of Bra c p, providing a scientific foundation for reducing the profilin allergens in food.

引用

页数：11