Hepatitis C Virus Polyprotein Processing
Hepatitis C Virus Polyprotein Processing
复制标题
丙型肝炎病毒多蛋白加工
DOI：
10.1007/978-4-431-68255-4_36
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
C. Rice
中科院分区：
文献类型：
--
作者：
A. Grakoui;D. Mccourt;C. Wychowski;Chao Lin;S. Feinstone;C. Rice
虽然HCV已被归类为黄病毒科，但对HCV多蛋白加工知之甚少。利用近全长菌株cDNA克隆和各种截短衍生物的表达研究已经映射了至少9个切割产物。这些包括推定的病毒粒子衣壳蛋白（C）、两种包膜糖蛋白（El和E2）和六种非结构蛋白（NS 2、NS 3、NS 4A、NS 4 B、NS 5A和NS 5 B）。通过缺失分析和定点突变鉴定并研究了HCV编码的两种重要的非结构区加工蛋白酶。位于NS 3蛋白N端三分之一的丝氨酸蛋白酶结构域被发现是必要的四个下游切割。在2/3位点的裂解似乎是自催化的，并由一种新的重叠蛋白酶NS 2和NS 3丝氨酸蛋白酶结构域组成的介导。这两种蛋白酶的切割位点已被定位的N-末端序列分析。
Although HCV has been classified in the flavivirus family, little is known about HCV polyprotein processing. Expression studies utilizing a nearly full-length strain cDNA clone and various truncated derivatives have mapped at least nine cleavage products. These include the putative virion capsid protein (C), two envelope glycoproteins (El and E2), and six nonstructural proteins (NS2, NS3, NS4A, NS4B, NS5A and NS5B). Two HCV-encoded proteinases important for non-structural region processing were identified and studied by deletion analyses and site-directed mutagenesis. A serine proteinase domain located in the N-terminal one third of the NS3 protein was found to be necessary for four downstream cleavages. Cleavage at the 2/3 site appeared to be autocatalytic and mediated by a novel overlapping proteinase consisting of NS2 and the NS3 serine proteinase domain. Cleavage sites for both proteinases have been localized by N-terminal sequence analysis.
DOI：
10.1073/pnas.90.22.10583
发表时间：
1993-11-15
影响因子：
11.1
作者：
GRAKOUI, A;MCCOURT, DW;RICE, CM
通讯作者：
RICE, CM