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• W2072462322 abstract "The serine proteinase of hepatitis C virus (HCV) non-structural protein NS3 was efficiently expressed in an active form as a fused protein with oligohistidine in Escherichia coli. The recombinant fusion protein was purified to near homogeneity by affinity chromatography on a metal chelation column. Trans-cleavage activity of this protein was investigated by using the substrate NS5 protein expressed in insect cells. The purified serine proteinase trans-cleaved the partially purified NS5 protein. In contrast, the NS3 proteins with mutations at the proposed catalytic site, Ser1165 or His1083, lost the trans-cleavage activity. Analysis of the authentic enzyme and variants with site-directed mutations provides a useful tool for understanding the structure-function relationship of the NS3 serine proteinase. We then developed an in vivo trans-cleavage assay system by coexpression of the NS3 proteinase and the NS5 substrate in E coli, and examined the effect of known inhibitors of serine proteinase. Inhibition of its proteolytic activity by N-p-tosyl-L-lysine chloromethyl ketone (TLCK) was observed, but only at high concentrations. The in vitro and in vivo trans-cleavage assays for NS3 serine proteinase will facilitate efficient testing for inhibitors of the replication of HCV and specific treatment for hepatitis C." @default.
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• W2072462322 date "1995-12-01" @default.
• W2072462322 modified "2023-10-14" @default.
• W2072462322 title "Proteolytic activity of NS3 serine proteinase of hepatitis C virus efficiently expressed inescherichia coli" @default.
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• W2072462322 doi "https://doi.org/10.1002/hep.1840220606" @default.
• W2072462322 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7489969" @default.
• W2072462322 hasPublicationYear "1995" @default.
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