Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein
Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein
复制标题
SARS-CoV膜蛋白的膜拓扑、N-糖基化和功能研究
作者：
D. Voss;S. Pfefferle;C. Drosten;Lea Stevermann;E. Traggiai;A. Lanzavecchia;S. Becker
严重急性呼吸综合征相关冠状病毒（SARS-CoV）的糖基化膜蛋白M是病毒粒子的主要结构成分，介导病毒粒子的组装和出芽。SARS-CoV M的膜拓扑结构及其N-糖基化的功能意义尚未完全了解，其与表面糖蛋白S的相互作用也未完全了解。利用生物化学和免疫荧光分析，我们发现M由一个短的糖基化的N-末端胞外域，三个跨膜段和一个长的，免疫原性的C-末端胞内域。虽然M的N-糖基化位点在1组和3组冠状病毒之间似乎是高度保守的，但使用表达糖基化缺陷M的重组SARS CoV的研究表明，M的N-糖基化既不影响病毒粒子的形状，也不影响它们在细胞培养中的感染性。截短的M蛋白的进一步的功能分析表明，N-末端134个氨基酸组成的三个跨膜结构域是足以介导的积累M在高尔基复合体和强制招聘的病毒刺突蛋白S的网站的病毒组装和出芽的ERGIC。
The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC.
DOI：
10.1073/pnas.87.18.6944
发表时间：
1990-09-01
影响因子：
11.1
作者：
MACHAMER, CE;MENTONE, SA;FARQUHAR, MG
通讯作者：
FARQUHAR, MG