In trans interaction of hepatitis C virus helicase domains mediates protease activity critical for internal NS3 cleavage and cell transformation |
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| Authors: | Ren-You Pan Yi-Hen Kou Ming-Fu Chang |
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| Affiliation: | a Institute of Microbiology, National Taiwan University College of Medicine, Taipei, Taiwan
b Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, Taipei, Taiwan |
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| Abstract: | Hepatitis C virus (HCV) internal non-structural protein 3 (NS3) cleavage can occur in trans in the presence of NS4A. In this study, we have further demonstrated a critical role of the helicase domain in the internal NS3 cleavage, different from HCV polyprotein processing which requires only the serine protease domain. The NTPase domain of NS3 helicase interacts with the RNA binding domain to facilitate internal NS3 cleavage. In addition, NS3 protease activity contributes to the transforming ability of the major internal cleavage product NS3(1-402). These findings imply important roles of the internal cleavage and protease activity of the NS3 protein in the pathogenesis of HCV.Structured summaryMINT-7306465: NS3 (uniprotkb:P29846) physically interacts (MI:0915) with NS3 (uniprotkb:P29846) by anti tag coimmunoprecipitation (MI:0007). |
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| Keywords: | Hepatitis C virus Internal NS3 cleavage In trans interaction NS3 helicase NS3 serine protease Polyprotein processing Transforming activity |
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