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

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 dr...

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Published inThe 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
LanguageEnglish
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
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Abstract 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.
AbstractList 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.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.
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.
Author Sharma, Suresh D.
Cameron, Craig E.
Raney, Kevin D.
Moustafa, Ibrahim M.
Author_xml – sequence: 1
  givenname: Kevin D.
  surname: Raney
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  email: raneykevind@uams.edu
  organization: From the Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205 and
– sequence: 2
  givenname: Suresh D.
  surname: Sharma
  fullname: Sharma, Suresh D.
  organization: the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802
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  givenname: Ibrahim M.
  surname: Moustafa
  fullname: Moustafa, Ibrahim M.
  organization: the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802
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  givenname: Craig E.
  surname: Cameron
  fullname: Cameron, Craig E.
  email: cec9@psu.edu
  organization: the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802
BackLink https://www.ncbi.nlm.nih.gov/pubmed/20457607$$D View this record in MEDLINE/PubMed
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Issue 30
Keywords Enzyme Mechanisms
Non-structural Protein 3 (NS3)
RNA Helicase
Hepatitis Virus
Protease
Hepatitis C Virus (HCV)
Antiviral Agents
Language English
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Snippet Hepatitis C virus non-structural protein 3 contains a serine protease and an RNA helicase. Protease cleaves the genome-encoded polyprotein and inactivates...
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SubjectTerms 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
Title Hepatitis C Virus Non-structural Protein 3 (HCV NS3): A Multifunctional Antiviral Target
URI https://dx.doi.org/10.1074/jbc.R110.125294
https://www.ncbi.nlm.nih.gov/pubmed/20457607
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https://pubmed.ncbi.nlm.nih.gov/PMC2906261
Volume 285
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