%0 Journal Article %T Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection. %+ Institut Armand Frappier (INRS-IAF) %+ Department of Biochemistry and Molecular Biology %+ Infectious Diseases %A Guévin, Carl %A Manna, David %A Bélanger, Claudia %A Konan, Kouacou V %A Mak, Paul %A Labonté, Patrick %Z This work was supported by NSERC of Canada (grant no. 312225-05). C. G. and C. B. were supported by a fellowship from the Armand-Frappier Foundation (Canada) %< avec comité de lecture %@ 0042-6822 %J Virology %I Elsevier %V 405 %N 1 %P 1-7 %8 2010-09-15 %D 2010 %R 10.1016/j.virol.2010.05.032 %M 20580051 %Z Life Sciences [q-bio]/Human health and pathology/Infectious diseasesJournal articles %X Autophagy is an important cellular process by which ATG5 initiates the formation of double membrane vesicles (DMVs). Upon infection, DMVs have been shown to harbor the replicase complex of positive-strand RNA viruses such as MHV, poliovirus, and equine arteritis virus. Recently, it has been shown that autophagy proteins are proviral factors that favor initiation of hepatitis C virus (HCV) infection. Here, we identified ATG5 as an interacting protein for the HCV NS5B. ATG5/NS5B interaction was confirmed by co-IP and metabolic labeling studies. Furthermore, ATG5 protein colocalizes with NS4B, a constituent of the membranous web. Importantly, immunofluorescence staining demonstrated a strong colocalization of ATG5 and NS5B within perinuclear regions of infected cells at 2 days postinfection. However, colocalization was completely lacking at 5DPI, suggesting that HCV utilizes ATG5 as a proviral factor during the onset of viral infection. Finally, inhibition of autophagy through ATG5 silencing blocks HCV replication. %G English %L pasteur-00819569 %U https://riip.hal.science/pasteur-00819569 %~ RIIP %~ INRS-IAF