Tanji Y, Hijikata M, Hirowatari Y, Shimotohno K
Virology Division, National Cancer Center Research Institute, Tokyo, Japan.
Gene. 1994 Aug 5;145(2):215-9. doi: 10.1016/0378-1119(94)90008-6.
A serine proteinase, Cpro-2, encoded in the hepatitis C virus (HCV) genome, is considered to be located in the N-terminal part of HCV p70, one of the putative nonstructural (NS) proteins of HCV. Cpro-2 is suggested to be responsible for producing several kinds of NS proteins by processing of the HCV precursor polyprotein. We identified the active domain of Cpro-2 and clarified the mechanism of HCV polyprotein processing; various HCV mutants deleted around this serine proteinase structure were cosynthesized with unprocessed HCV polypeptides containing Cpro-2-dependent cleavage sites in COS-1 cells. We showed that Cpro-2 cleaved the HCV precursor polyprotein intermolecularly (trans) and that Cpro-2 domain which is necessary and sufficient for that cleavage mapped to within 167 aa, from Gly1049 to Ser1215 of the HCV precursor polyprotein.
一种在丙型肝炎病毒（HCV）基因组中编码的丝氨酸蛋白酶Cpro-2，被认为位于HCV p70的N端部分，HCV p70是HCV一种假定的非结构（NS）蛋白。Cpro-2被认为通过加工HCV前体多蛋白来产生几种NS蛋白。我们鉴定了Cpro-2的活性结构域，并阐明了HCV多蛋白加工机制；在COS-1细胞中，将此丝氨酸蛋白酶结构周围缺失的各种HCV突变体与含有Cpro-2依赖性切割位点的未加工HCV多肽共合成。我们发现Cpro-2以分子间（反式）方式切割HCV前体多蛋白，并且对于该切割必要且充分的Cpro-2结构域定位于HCV前体多蛋白的167个氨基酸范围内，即从Gly1049到Ser1215。
