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Journal of Virology, November 2009, p. 11378-11384, Vol. 83, No. 21
0022-538X/09/$08.00+0     doi:10.1128/JVI.01122-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

An Amphipathic {alpha}-Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane Association {triangledown} ,{dagger}

Jérôme Gouttenoire,1 Roland Montserret,2 Audrey Kennel,1 François Penin,2 and Darius Moradpour1*

Division of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, University of Lausanne, CH-1011 Lausanne, Switzerland,1 Institut de Biologie et Chimie des Protéines, UMR 5086, CNRS, University of Lyon, IFR128 BioSciences Gerland-Lyon Sud, F-69367 Lyon, France2

Received 2 June 2009/ Accepted 10 August 2009

Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic {alpha}-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.

* Corresponding author. Mailing address: Division of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, BU44/07/2421, Rue du Bugnon 44, CH-1011 Lausanne, Switzerland. Phone: 41 21 314 47 23. Fax: 41 21 314 47 18. E-mail: Darius.Moradpour{at}chuv.ch

{triangledown} Published ahead of print on 19 August 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, November 2009, p. 11378-11384, Vol. 83, No. 21
0022-538X/09/$08.00+0     doi:10.1128/JVI.01122-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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