乙型肝炎病毒表面大蛋白N-糖基化修饰对内质网应激的影响  

The N-glycosylation of large surface protein of HBV affects the endoplasmic reticulum stress

作　　者：夏正林[1] 萧金丰[1] 王汉宁[1] 陈开运[1] 贺轲[1] 段小鹏[1] 陈京龙[2] 向国安[1] 

机构地区：[1]南方医科大学附属广东省第二人民医院普外科,广州510515 [2]首都医科大学附属北京地坛医院

出　　处：《国际病毒学杂志》2014年第2期58-62,共5页International Journal of Virology

基　　金：国家自然科学基金（81071990、81201758）;广州市科技计划项目（2011J410010、2011J4300066）

摘　　要：目的 研究乙型肝炎病毒表面大蛋白（large surface protein of HBV,LHBs）N-糖基化修饰对内质网应激的影响.方法 将LHBs基因进行单点突变,检测野生型LHBs和突变型LHBs对内质网应激和EAED路径相关蛋白表达的影响.检测LHBs与多种泛素链的结合状态,确定LHBs的糖基化基序.结果 LHBs N-糖基化修饰与内质网应激有关.N15S、N123S、N177S位点突变的LHBs可以诱导L02细胞过表达EDEM.野生型LHBs和突变型LHBs均包含有P62衍生的UBA结合域.结论 LHBs N-糖基化修饰可以调节内质网应激.N320K可能是LHBs N-糖基化修饰的关键位点.Objective To understand the effects of the N-glycosylation modification of LHBs （ large surface protein of HBV） on the endoplasmic reticulum stress. Methods The LHBs was mutated, and the endoplasmic reticulum stress and EAED path of cells transfected with LHBs and its mutations was evaluated. LHBs proteins bound to multi-ubiquitin chains and its glycosylation motif were studied. Results These da- ta demonstrated that the N-glycosylation motifs of LHBs were related to ER stress. The N15S, N123S and N177S mutated LHBs proteins could induce over-expression of EDEM in L02 cells. LHBs and its mutated proteins contained p62-dcrived UBA domain. Conclusions Our results strongly suggested that the N-glyco- sylation modification of LHBs affects the ER stress. The N320K may be the key sites N-linked glycosylatiou modification of LHBs.

关 键 词：乙型肝炎病毒 糖基化 内质网应激 细胞增殖 

分 类 号：R512.62[医药卫生—内科学]