Hepatitis C virus infection B.J. Thomson, R.G. Finch  Clinical Microbiology and Infection  Volume 11, Issue 2, Pages 86-94 (February 2005) DOI: 10.1111/j.1469-0691.2004.01061.x Copyright © 2005 European Society of Clinical Infectious Diseases Terms and Conditions

Fig. 1 The structure of the hepatitis C virus genome [7]. The 5’ non-coding region (NCR) contains four highly conserved RNA domains and an internal ribosome entry site. Structural proteins include core, which forms the virus capsid, and the envelope glycoproteins E1 and E2. The structural proteins are separated from the non-structural (NS) proteins by a short peptide, P7 (not shown). NS proteins are designated NS2 to NS5. NS4 and NS5 are each processed further into two subunits, A and B. NS2 is a component of the NS2–NS3 metalloprotease that autocatalyses cleavage of the NS2–NS3 junction; NS3 contributes to the NS2–NS3 protease and contains a separate serine protease that acts with co-factor NS4A to release the remaining NS proteins. The C-terminal region of NS3 contains an RNA helicase and nucleotide triphosphatase activity required for virus replication. NS5B is the RNA-dependent RNA polymerase. The functions of NS4B and NS5A in the virus life-cycle are unknown. The 3'-NCR contains a series of stable RNA stem–loop structures and a polypyrimidine tract that is essential for genome replication. Clinical Microbiology and Infection 2005 11, 86-94DOI: (10.1111/j.1469-0691.2004.01061.x) Copyright © 2005 European Society of Clinical Infectious Diseases Terms and Conditions