Biochemical analysis of the secreted and virion glycoproteins of Ebola virus
Biochemical analysis of the secreted and virion glycoproteins of Ebola virus
复制标题
DOI：
10.1128/jvi.72.8.6442-6447.1998
复制
发表时间：
1998-08-01
影响因子：
5.4
通讯作者：
Peters, CJ
中科院分区：
文献类型：
--
作者：
Sanchez, A;Yang, ZY;Peters, CJ
我们分析了扎伊尔种埃博拉病毒表达的糖蛋白的切割、寡聚化和其他结构特性，以更好地确定其功能。分泌50- 70 kda和150 kda的病毒粒子/结构糖蛋白（分别为SGP和GP）共享295个N端残基，在N端附近被信号酶切割。第二次切割事件发生在GP的多碱基位点（RRTRR向下箭头），可能由furin介导，导致两个糖蛋白（GP1和GP2）通过二硫键连接。在所有埃博拉病毒的gp中，该furin切割位点位于相同位置（R[R/K]X[R/K]R向下箭头），在马尔堡病毒中预测有一个（R[R/K]KR向下箭头），尽管位置不同。根据交联研究的结果，我们能够确定埃博拉病毒粒子聚合体由GP1-GP2异二聚体三聚体组成，其结构的各个方面与逆转录病毒、副粘病毒和流感病毒相似。我们还确定，SGP几乎完全以二硫键连接的同型二聚体的形式从感染细胞分泌。
The glycoproteins expressed by a Zaire species of Ebola virus were analyzed for cleavage, oligomerization, and other structural properties to better define their functions. The 50- to 70-kDa secreted and 150-kDa virion/structural glycoproteins (SGP and GP, respectively), which share the 295 N-terminal residues, are cleaved near the N terminus by signalase, A second cleavage event, occurring in GP at a multibasic site (RRTRR down arrow) that is likely mediated by furin, results in two glycoproteins (GP1 and GP2) linked by disulfide bonding. This furin cleavage site is present in the same position in the GPs of all Ebola viruses (R[R/K]X[R/K]R down arrow), and one is predicted for Marburg viruses (R[R/K]KR down arrow), although in a different location. Based on the results of cross-linking studies, we were able to determine that Ebola virion peplomers are composed of trimers of GP1-GP2 heterodimers and that aspects of their structure are similar to those of retroviruses, paramyxoviruses, and influenza viruses. We also determined that SGP is secreted from infected cells almost exclusively in the form of a homodimer that is joined by disulfide bonding.