Abstract
We identified an N-terminal amphipathic helix (AH) in one of hepatitis C virus (HCV)'s nonstructural proteins, NS5A. This AH is necessary and sufficient for membrane localization and is conserved across isolates. Genetically disrupting the AH impairs HCV replication. Moreover, an AH peptide-mimic inhibits the membrane association of NS5A in a dose-dependent manner. These results have exciting implications for the HCV life cycle and novel antiviral strategies.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Cell Line
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Cell Membrane / metabolism
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Cell Membrane / virology
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Conserved Sequence
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Gene Expression Regulation, Viral*
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Hepacivirus / genetics
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Hepacivirus / physiology*
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Humans
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Peptides / chemical synthesis
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Peptides / chemistry
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RNA, Viral / biosynthesis*
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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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Peptides
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RNA, Viral
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Viral Nonstructural Proteins
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NS-5 protein, hepatitis C virus