牡蛎热休克蛋白70吸附人源诺如病毒功能域的解析  

Analysis of the Functional Domain of Oyster Heat Shock Protein 70 that Binds to Human Norovirus

作　　者：王艳飞 张子蕾 罗广达 李静雯 王大鹏[1] WANG Yanfei;ZHANG Zilei;LUO Guangda;LI Jingwen;WANG Dapeng(Department of Food Science and Technology,School of Agriculture and Biology,Shanghai Jiao Tong University,Shanghai 200240,China;Department of Inspection and Quarantine Technical Communication,Shanghai Customs College,Shanghai 200120,China)

机构地区：[1]上海交通大学农业与生物学院食品科学与工程系,上海200240 [2]上海海关学院检验检疫技术交流部,上海200120

出　　处：《病毒学报》2023年第2期393-400,共8页Chinese Journal of Virology

基　　金：国家自然基金面上项目(项目号:32072319),题目:牡蛎热休克蛋白70与人源诺如病毒动态互作的分子机制。

摘　　要：人源诺如病毒(Human norovirus,HuNoV)是全球范围内最重要的食源性病毒之一,牡蛎是其主要的食源性传播载体。已有研究发现:牡蛎热休克蛋白70(oyster Heat shock protein 70,oHSP70)可吸附不同基因型HuNoV,但oHSP70吸附病毒的功能域不清楚。本研究对oHSP70的N端和C端分别进行克隆表达纯化,并采用ELISA方法测定其与不同基因型HuNoV主要衣壳蛋白P功能域的结合能力。实验结果表明:成功获得N端和C端oHSP70的原核表达产物;N端oHSP70与不同基因型HuNoV P蛋白结合能力显著强于C端(P<0.05)。因此,N端oHSP70是结合HuNoV P蛋白的主要结构域。本研究结果为进一步揭示oHSP70与HuNoV互作的分子机制提供了理论支撑。Human norovirus(HuNoV) is one of the most important food-borne viruses worldwide. Oysters are the main vector of HuNoV. Previously, we found that oyster heat shock protein 70(oHSP70) could bind to different genotypes of HuNoV. However, the functional domain of oHSP70 involved in adsorbing virus remains unclear. In this work, the N-terminal and C-terminal of oHSP70 were cloned and purified separately, and the ability to bind the functional domain of the major coat protein P of HuNoV was determined by ELISA. Results showed that the N-terminal and C-terminal oHSP70 products were successfully obtained. ELISA results showed that the N-terminal oHSP70 domain bound significantly stronger than the C-terminal domain to the HuNoV P protein(P <0.05). The N-terminal oHSP70 domain is the main structural domain binding to the HuNoV P protein, which provides theoretical support for further analysis of the interaction between oHSP70and HuNoV.

关 键 词：人源诺如病毒 牡蛎 热休克蛋白70 配体 原核表达 

分 类 号：Q939.99[生物学—微生物学]