Analysis of Immunoreactivity of α/α2-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics
Analysis of Immunoreactivity of α/α2-Tropomyosin from Haliotis discus hannai, Based on IgE Epitopes and Structural Characteristics
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基于IgE表位和结构特征的皱纹盘鲍α/α2-原肌球蛋白的免疫反应性分析
DOI：
10.1021/acs.jafc.1c06401
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发表时间：
2021
影响因子：
6.1
通讯作者：
Guang-Ming Liu
中科院分区：
文献类型：
--
作者：
Nai-Ru Ji;Xin-Yu Han;Chen-Chen Yu;Yu-Jia Wang;Xin-Rong He;Hong Liu;Fei Huan;Dong Lai;Min-Jie Cao;Guang-Ming Liu
原肌球蛋白（tromyosin， TM）被报道为贝类的超级线圈过敏原。然而，关于其结构与致敏性之间的联系的信息很少。本研究从铁饼中鉴定出了TM亚基（α-TM）和TM超螺旋（α2-TM）。α2-TM的免疫反应性高于α-TM。同时，对α-TM和α2-TM的7个线性表位进行了验证，并对α2-TM的2个构象表位进行了预测。理化性质和化学键分析证实α2-TM中存在二硫键。光谱和疏水性分析表明，α-TM比α2-TM表现出更高的α-螺旋特征和荧光强度峰的蓝移。结构分析揭示了α2-TM中存在构象表位的可能性，可以进一步解释α-TM与α2-TM之间的免疫反应性差异。这些结果提高了对鲍鱼的认识，为鲍鱼的食品加工奠定了基础。
Tropomyosin (TM) was reported to be a supercoil allergen of shellfish. However, little information is available about its link between structure and allergenicity. In this study, the subunit of TM (α-TM) and supercoil of TM (α2-TM) were identified fromHaliotis discus hannai. α2-TM showed higher immunoreactivity than α-TM. Meanwhile, seven linear epitopes in α-TM and α2-TM were verified, and two conformational epitopes in α2-TM were predicted. The physicochemical properties and chemical bond assays confirmed the existence of the disulfide bond in α2-TM. According to spectroscopy and hydrophobicity analysis, α-TM showed higher α-helix features and blueshift of the fluorescence intensity peak compared with those of α2-TM. The structure analysis revealed the possibility of conformational epitopes in α2-TM, which could explain the immunoreactivity differences between α-TM and α2-TM further. These results improved the understanding ofHaliotis discus hannaiTM, which lay the foundation for the food processing of abalone.