Abstract
Hepatitis C virus (HCV) NS3-4A is required for viral replication and assembly. We establish that virus assembly is sensitive to mutations in the linker region between the helicase and protease domains of NS3-4A. However, we find that the protease cleavage, RNA binding, and unwinding rates of NS3 are minimally affected in vitro. Thus, we conclude that the NS3 linker is critical for mediating protein-protein interactions and dynamic control rather than for modulating the enzymatic functions of NS3-4A.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Hepacivirus / chemistry
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Hepacivirus / enzymology*
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Hepacivirus / genetics
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Hepacivirus / physiology*
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Hepatitis C / virology*
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Humans
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Intracellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Protein Binding
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Sequence Alignment
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Viral Nonstructural Proteins / chemistry*
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / metabolism*
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Virus Replication*
Substances
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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NS3 protein, hepatitis C virus
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NS4A cofactor peptide, Hepatitis C virus
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Viral Nonstructural Proteins