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J Virol. 2009 Nov;83(21):11378-84. doi: 10.1128/JVI.01122-09. Epub 2009 Aug 19.

An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.

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1
Division of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, BU44/07/2421, Rue du Bugnon 44, CH-1011 Lausanne, Switzerland.

Abstract

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.

PMID:
19692468
PMCID:
PMC2772773
DOI:
10.1128/JVI.01122-09
[Indexed for MEDLINE]
Free PMC Article
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