Hepatitis C Virus Non-structural Protein 3 (HCV NS3): A Multifunctional Antiviral Target

• Published in: The Journal of biological chemistry Vol. 285; no. 30; pp. 22725 - 22731
• Main Authors: Raney, Kevin D., Sharma, Suresh D., Moustafa, Ibrahim M., Cameron, Craig E.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.07.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Antiviral Agents; Antiviral Agents - metabolism; Antiviral Agents - pharmacology; Enzyme Mechanisms; Hepacivirus - metabolism; Hepatitis C virus; Hepatitis C Virus (HCV); Hepatitis Virus; Immunity, Innate - immunology; Microbiology; Minireviews; Non-structural Protein 3 (NS3); Nucleic Acids - chemistry; Nucleic Acids - metabolism; Protease; Protein Multimerization; RNA Helicase; Viral Nonstructural Proteins - antagonists & inhibitors; Viral Nonstructural Proteins - chemistry; Viral Nonstructural Proteins - immunology; Viral Nonstructural Proteins - metabolism; Enzyme Mechanisms; Non-structural Protein 3 (NS3); RNA Helicase; Hepatitis Virus; Protease; Hepatitis C Virus (HCV); Antiviral Agents
• ISSN: 0021-9258; 1083-351X; 1083-351X
• DOI: 10.1074/jbc.R110.125294

Hepatitis C virus non-structural protein 3 contains a serine protease and an RNA helicase. Protease cleaves the genome-encoded polyprotein and inactivates cellular proteins required for innate immunity. Protease has emerged as an important target for the development of antiviral therapeutics, but drug resistance has turned out to be an obstacle in the clinic. Helicase is required for both genome replication and virus assembly. Mechanistic and structural studies of helicase have hurled this enzyme into a prominent position in the field of helicase enzymology. Nevertheless, studies of helicase as an antiviral target remain in their infancy.