CAJ | 학술논문

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.
목적 연구을형간염병독표면대단백(large surface protein of HBV,LHBs)N-당기화수식대내질망응격적영향.방법 장LHBs기인진행단점돌변,검측야생형LHBs화돌변형LHBs대내질망응격화EAED로경상관단백표체적영향.검측LHBs여다충범소련적결합상태,학정LHBs적당기화기서.결과 LHBs N-당기화수식여내질망응격유관.N15S、N123S、N177S위점돌변적LHBs가이유도L02세포과표체EDEM.야생형LHBs화돌변형LHBs균포함유P62연생적UBA결합역.결론 LHBs N-당기화수식가이조절내질망응격.N320K가능시LHBs N-당기화수식적관건위점.
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 data 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-derived UBA domain.Conclusions Our results strongly suggested that the N-glycosylation modification of LHBs affects the ER stress.The N320K may be the key sites N-linked glycosylation modification of LHBs.