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Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication.


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.

SUBMITTER: Elazar M 

PROVIDER: S-EPMC154017 | biostudies-literature | 2003 May

REPOSITORIES: biostudies-literature

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Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication.

Elazar Menashe M   Cheong Kwang Ho KH   Liu Ping P   Greenberg Harry B HB   Rice Charles M CM   Glenn Jeffrey S JS  

Journal of virology 20030501 10


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. ...[more]

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