![]() This suggests therefore that efficient cleavage at the NS2/NS3 junction is a pivotal event in HCV replication. ![]() Furthermore, the presence of uncleaved NS2 sequences on the enzyme severely impeded NS3-mediated proteolysis at downstream sites in the polyprotein. However, efficient cleavage at this position was dependent on the prior removal of the NS2 protein. Time-course analysis of the proteolytic processing of the HCV non-structural pre-cursor showed that the cis cleavage between NS3 and NS4 occurred extremely rapidly. ![]() However, processing at the other predicted sites of NS3-mediated cleavage varied mark-edly in efficiency, the site most susceptible being that between NS5A and NS5B. We confirmed that expression of the NS3-5 polyprotein in rabbit reticulo-cyte lysates results in efficient cis processing at the NS3/NS4 junction. The protease activity of the hepatitis C virus (HCV) NS3 protein has been investigated using transient expression methods in mammalian cells, as well as in vitro transcription/translation systems. ![]()
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January 2023
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