The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation
The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation
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DOI：
10.1016/j.foodchem.2019.125853
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发表时间：
2020-04-25
期刊：
影响因子：
8.8
通讯作者：
Tu, Zong-cai
中科院分区：
文献类型：
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作者：
Liu, Jun;Chen, Wen-mei;Tu, Zong-cai
牛乳清蛋白(α-Lac)过敏是常见的健康问题。本研究通过酶联免疫吸附试验、细胞实验和高分辨质谱仪对α-Lac蛋白修饰(糖基化、磷酸化和乙酰化)后的致敏反应性和结构性质进行了评价。三种改良方法均显著降低了α-Lac的IgE/Ig G结合量、组胺和IL-6的释放，并改变了α-Lac的构象结构。α-Lac分别在K13、K16、K94、K98和K108处糖化，在Y18、S22、Y103和S112处磷酸化，在K13、T33、S34、T38、S47、K62、S69、S70、K108和K114处乙酰化，从而掩盖了α-Lac的线性表位。因此，糖基化、磷酸化和乙酰化引起的α-Lac致敏反应性的降低不仅与其修饰部位的屏蔽作用有关，还与构象结构的变化有关。本研究证实了蛋白质修饰是一种很有前景的降低过敏蛋白致敏反应性的方法。
Bovine alpha-lactalbumin (alpha-Lac) allergy is a common health problem. This study assesses the allergenic reactivity and the structural properties of alpha-Lac after protein modification (glycation, phosphorylation and acetylation) by ELISA, cells experiment and high-resolution mass spectrometry. Three modified methods significantly reduced the IgE/IgG-binding capacity, and the release of histamine and interleukin-6, and changed the conformational structure of alpha-Lac. alpha-Lac was glycated at K13, K16, K94, K98, and K108, phosphorylated at Y18, S22, Y103, and S112, and acetylated at K13, T33, S34, T38, S47, K62, S69, S70, K108, and K114, respectively, leading to masking the linear epitopes of alpha-Lac. Therefore, the decrease of allergenic reactivity of alpha-Lac induced by glycation, phosphorylation and acetylation depends upon not only the shielding effect of their modified sites, but also the change of conformational structure. This study confirmed that protein modification was a promising method for decreasing the allergenic reactivity of allergic proteins.