Persistent infection with hepatitis C virus (HCV) is a common cause of chronic liver disease, including chronic hepatitis, cirrhosis, and hepatocellular carcinoma. HCV is an enveloped, single-stranded RNA virus with a 9.6-kb positive-polarity genome, which encodes a polyprotein precursor of about 3,000 amino acids. The HCV polyprotein is proteolytically processed by cellular and HCV proteases into at least 10 distinct products. NS3 serine protease and helicase as well as NS5B RNA-dependent RNA polymerase are believed to be components of a replication complex responsible for viral RNA replication and have been shown to be essential for the HCV replication in chimpanzees. These HCV enzymes have been the major targets for the development of HCV-specific therapeutics during the past decade. The HCV NS3/4A protease is responsible for cleavage at four sites within the HCV polyprotein to generate the N termini of the NS4A, NS4B, NS5A, and NS5B proteins. It has been shown that the central region (amino acids 21-30) of the 54-residue NS4A protein is essential and sufficient for the enhancement of proteolytic activity of the NS3 serine protease. In recent phase I trials, a 2-3-log reduction of HCV viral load was observed after a 2-day treatment with a serine protease inhibitor, which provided the first proof-of-concept evidence that HCV NS3/4A protease inhibitors could be a new therapeutic option for hepatitis C patients.
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In the United States, the annual number of newly acquired acute hepatitis C virus (HCV) infections has declined from an estimated 180,000 in the mid 1980s to an estimated 28,000 in 1995. Approximately 25% to 30% of these infections are
Journal of virology, 74(4), 2046-2051 (2000-01-22)
Hepatitis C virus (HCV) infection is a widespread major human health concern. Significant obstacles in the study of this virus include the absence of a reliable tissue culture system and a small-animal model. Recently, we constructed full-length HCV cDNA clones
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