摘要
目的通过研究中国马源P[12]型轮状病毒GST-VP8*-HorseP[12]E403蛋白与寡糖、唾液受体的结合特征,进而为轮状病毒的跨种传播及受体间的作用机制提供重要科学依据。方法通过大肠杆菌表达系统表达、纯化中国马源P[12]型轮状病毒GST-VP8*-Horse P[12]E403蛋白,并利用唾液及寡糖结合实验分析该基因型的受体结合特征。结果马源GST-VP8*-Horse P[12]E403蛋白与黏蛋白核心mucin core 2糖结合良好,与A、B、Lewis型等寡糖及唾液中的HBGAs均不结合。结论VP8*-Horse P[12]E403蛋白的潜在受体可能是黏蛋白核心2,未与人唾液发生结合。
Objective To study the binding characteristics of horse-derived P[12]rotavirus GST-VP8*-Horse P[12]E403 protein to oligosaccharides and saliva receptors,provides an important scientific basis for the cross-species transmission and the mechanism of interaction between the bodies.Methods The E.coli expression system was used to express and purify the horse-derived P[12]rotavirus GST-VP8*-Horse P[12]E403 protein.The receptor binding characteristics of this genotype were analyzed by saliva and oligosaccharide binding experiments.Results Horse-derived GST-VP8*-Horse P[12]E403 protein binds well with mucin core 2 sugar,but does not bind to other oligosaccharides such as A,B,Lewis,and HBGAs in saliva.Conclusions The potential receptor of VP8*-Horse P[12]E403 protein may be mucin core 2,and it did not bind to human saliva.
作者
王萌璇
张佳艳
曾秋艳
孙晓曼
章青
王宏
李丹地
段招军
Wang Mengxuan;Zhang Jiayan;Zeng Qiuyan;Sun Xiaoman;Zhang Qing;Wang Hong;Li Dandi;Duan Zhaojun(National Institute for Viral Disease Control and Prevention,Chinese Center for Diseases Control and Prevention,Beijing 102206,China;Department of Food and Chemical Engineering,Lushan College of Guangxi University of Science and Technology,Liuzhou 545000,China)
出处
《中华实验和临床病毒学杂志》
CAS
CSCD
2020年第3期309-312,共4页
Chinese Journal of Experimental and Clinical Virology
基金
国家自然科学基金(81601813)。