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The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity
Author(s) -
Parent Romain,
Qu Xiaoyu,
Petit MarieAnne,
Beretta Laura
Publication year - 2009
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.22852
Subject(s) - infectivity , hepatitis c virus , virology , virus , biology , heat shock protein , immunogold labelling , viral envelope , lipid droplet , antibody dependent enhancement , viral entry , viral replication , viral interference , hepatitis b virus , hepacivirus , antibody , microbiology and biotechnology , biochemistry , immunology , gene
There is growing evidence that virus particles contain host cell proteins. These proteins may provide viruses with means to evade the immune system or with mechanisms for cell entry and release. A proteomic analysis performed on highly purified hepatitis C virus (HCV) J6/JFH virions identified the heat shock cognate protein 70 (HSC70) as part of the viral particles. These results were further validated via immunogold electron microscopy. The HSC70 interaction HPD motif was found present on the E2 envelope of the J6/JFH strain, as well as in over 50% of genotype 2 clinical HCV isolates. In addition, HSC70 was found associated with viral particles from an HCV genotype 2a–infected patient. Preincubation of HCV particles with anti‐HSC70 antibodies decreased viral infectivity. Within infected cells, colocalization of HSC70 with the HCV core and E2 proteins was observed around lipid droplets. Reduction of HSC70 expression using an RNA interference approach decreased the volume of lipid droplets as well as viral release without affecting HCV replication levels. Conclusion: These results suggest that HSC70 modulates HCV infectivity and lipid droplet–dependent virus release. (H EPATOLOGY 2009.)