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Journal of Virology, May 2003, p. 6055-6061, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.6055-6061.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Amphipathic Helix-Dependent Localization of NS5A Mediates Hepatitis C Virus RNA Replication

Menashe Elazar,1 Kwang Ho Cheong,1,2 Ping Liu,1 Harry B. Greenberg,1,2,{dagger} Charles M. Rice,3 and Jeffrey S. Glenn1,2*

Division of Gastroenterology and Hepatology, Stanford University School of Medicine,1 Department of Microbiology and Immunology, Veterans Administration Medical Center, Palo Alto, California,2 Center for the Study of Hepatitis C, Rockefeller University, New York, New York3

Received 31 October 2002/ Accepted 7 February 2003

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.

* Corresponding author. Mailing address: Division of Gastroenterology and Hepatology, Stanford University School of Medicine, CCSR Building, Room 3115, 269 Campus Dr., Palo Alto, CA 94305-5187. Phone: (650) 725-3373. Fax: (650) 723-5488. E-mail: jeffrey.glenn{at}stanford.edu.

{dagger} Present address: Aviron, Inc., Mountain View, CA 94043.

Journal of Virology, May 2003, p. 6055-6061, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.6055-6061.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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