Palmitoylation and polymerization of hepatitis C virus NS4B protein.

Abstract:

:Hepatitis C Virus (HCV) NS4B protein induces a specialized membrane structure which may serve as the replication platform for HCV RNA replication. In the present study, we demonstrated that NS4B has lipid modifications (palmitoylation) on two cysteine residues (cysteines 257 and 261) at the C-terminal end. Site-specific mutagenesis of these cysteine residues on individual NS4B proteins and on an HCV subgenomic replicon showed that the lipid modifications, particularly of Cys261, are important for protein-protein interaction in the formation of the HCV RNA replication complex. We further demonstrated that NS4B can undergo polymerization. The main polymerization determinants were mapped in the N-terminal cytosolic domain of NS4B protein; however, the lipid modifications on the C terminus also facilitate the polymerization process. The lipid modification and the polymerization activity could be two properties of NS4B important for its induction of the specialized membrane structure involved in viral RNA replication.

journal_name

J Virol

journal_title

Journal of virology

authors

Yu GY,Lee KJ,Gao L,Lai MM

doi

10.1128/JVI.00053-06

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

6013-23

issue

12

eissn

0022-538X

issn

1098-5514

pii

80/12/6013

journal_volume

80

pub_type

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