Nonstructural 5A protein of hepatitis C virus regulates heat shock protein 72 for its own propagation

We identified heat shock protein 72 (Hsp72) as a host factor that was differentially expressed in cells expressing nonstructural 5A (NS5A) protein. To investigate how NS5A modulates Hsp72 in hepatitis C virus (HCV) life cycle, we examined the role of Hsp72 in HCV replication and virus production. NS...

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Bibliographic Details
Published in:Journal of viral hepatitis 2012-05, Vol.19 (5), p.353-363
Main Authors: Lim, Y. S., Shin, K. S., Oh, S. H., Kang, S. M., Won, S. J., Hwang, S. B.
Format: Article
Language:English
Subjects:
Acetylcysteine
Cell Line
Data processing
Glutathione
heat shock protein 72
Heat shock proteins
Hepacivirus - pathogenicity
Hepatitis C virus
hepatocellular carcinoma
Hepatocytes - virology
Host-Pathogen Interactions
HSP72 Heat-Shock Proteins - metabolism
Hsp72 protein
Humans
Life cycle
NF-AT protein
NFAT5
nonstructural 5A
NS5A protein
Reactive oxygen species
Replication
RNA
RNA viruses
Transcription factors
Transcription Factors - metabolism
Viral Nonstructural Proteins - metabolism
Virus Replication
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Summary:We identified heat shock protein 72 (Hsp72) as a host factor that was differentially expressed in cells expressing nonstructural 5A (NS5A) protein. To investigate how NS5A modulates Hsp72 in hepatitis C virus (HCV) life cycle, we examined the role of Hsp72 in HCV replication and virus production. NS5A specifically interacted with Hsp72. Both Hsp72 and nuclear factor of activated T cells 5 (NFAT5) levels were increased in cells expressing NS5A protein. Treatments of N‐acetylcysteine and glutathione markedly reduced protein levels of both NFAT5 and Hsp72. Knockdown of NFAT5 resulted in decrease in Hsp72 level in cells expressing NS5A. Importantly, silencing of Hsp72 expression resulted in decrease in both RNA replication and virus production in HCV‐infected cells. These data indicate that NS5A modulates Hsp72 via NFAT5 and reactive oxygen species activation for HCV propagation.
ISSN:1352-0504
1365-2893
DOI:10.1111/j.1365-2893.2011.01556.x