Literature DB >> 12719597

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

Menashe Elazar1, Kwang Ho Cheong, Ping Liu, Harry B Greenberg, Charles M Rice, Jeffrey S Glenn.   

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.

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Year:  2003        PMID： 12719597      PMCID： PMC154017          DOI： 10.1128/jvi.77.10.6055-6061.2003

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


  44 in total

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Journal:  Gene       Date:  1996-12-05       Impact factor: 3.688

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Journal:  Virology       Date:  1997-04-14       Impact factor: 3.616
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  73 in total

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Review 5.  A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication.

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7.  A virocidal amphipathic {alpha}-helical peptide that inhibits hepatitis C virus infection in vitro.

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8.  A nucleotide binding motif in hepatitis C virus (HCV) NS4B mediates HCV RNA replication.

Authors:  Shirit Einav; Menashe Elazar; Tsafi Danieli; Jeffrey S Glenn
Journal:  J Virol       Date:  2004-10       Impact factor: 5.103

9.  An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication.

Authors:  Menashe Elazar; Ping Liu; Charles M Rice; Jeffrey S Glenn
Journal:  J Virol       Date:  2004-10       Impact factor: 5.103

10.  TARGETING THE NS5A PROTEIN OF HCV: AN EMERGING OPTION.

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