Role of oxysterol binding protein in hepatitis C virus infection.

Abstract:

:Hepatitis C virus (HCV) RNA genome replicates within the ribonucleoprotein (RNP) complex in the modified membranous structures extended from endoplasmic reticulum. A proteomic analysis of HCV RNP complexes revealed the association of oxysterol binding protein (OSBP) as one of the components of these complexes. OSBP interacted with the N-terminal domain I of the HCV NS5A protein and colocalized to the Golgi compartment with NS5A. An OSBP-specific short hairpin RNA that partially downregulated OSBP expression resulted in a decrease of the HCV particle release in culture supernatant with little effect on viral RNA replication. The pleckstrin homology (PH) domain located in the N-terminal region of OSBP targeted this protein to the Golgi apparatus. OSBP deletion mutation in the PH (DeltaPH) domain failed to localize to the Golgi apparatus and inhibited the HCV particle release. These studies suggest a possible functional role of OSBP in the HCV maturation process.

journal_name

J Virol

journal_title

Journal of virology

authors

Amako Y,Sarkeshik A,Hotta H,Yates J 3rd,Siddiqui A

doi

10.1128/JVI.00958-09

subject

Has Abstract

pub_date

2009-09-01 00:00:00

pages

9237-46

issue

18

eissn

0022-538X

issn

1098-5514

pii

JVI.00958-09

journal_volume

83

pub_type

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