Abstract
Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is required for HCV polyprotein processing and particle assembly. It comprises an N-terminal membrane domain and a C-terminal, cytosolically oriented protease domain. Here, we demonstrate that the NS2 protease domain itself associates with cellular membranes. A single charged residue in the second α-helix of the NS2 protease domain is required for proper membrane association, NS2 protein stability, and efficient HCV polyprotein processing.
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.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Cell Membrane / metabolism*
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Green Fluorescent Proteins
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Hepacivirus / enzymology*
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Microscopy, Confocal
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Models, Molecular*
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Molecular Sequence Data
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Protein Structure, Tertiary / genetics
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Sequence Analysis, DNA
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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 Assembly / genetics
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Virus Assembly / physiology*
Substances
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NS2 protein, Hepatitis C virus
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Viral Nonstructural Proteins
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Green Fluorescent Proteins