LARP1 binding to hepatitis C virus particles is correlated with intracellular retention of viral infectivity - CRCL-Epigénetique et épigénomique des carcinomes viro-induits Accéder directement au contenu
Article Dans Une Revue Virus Research Année : 2019

LARP1 binding to hepatitis C virus particles is correlated with intracellular retention of viral infectivity

Résumé

Hepatitis C virus (HCV) virions contain a subset of host liver cells proteome often composed of interesting virus-interacting factors. A proteomic analysis performed on double gradient-purified clinical HCV highlighted the translation regulator LARP1 on these virions. This finding was validated using post-virion capture and immunoelectron microscopy, as well as immunoprecipitation applied to in vitro (Huh7.5 liver cells) grown (Gt2a, JFH1 strain) and patient-derived (Gt1a) HCV particles. Upon HCV infection of Huh7.5 cells, we observed a drastic transfer of LARP1 to lipid droplets, inducing colocalization with core proteins. RNAi-mediated depletion of LARP1 using the C911 control approach decreased extracellular infectivity of HCV Gt1a (H77), Gt2a (JFH1), and Gt3a (S52 chimeric strain), yet increased their intracellular infectivity. This latter effect was unrelated to changes in the hepatocyte secretory pathway, as evidenced using a functional RUSH assay. These results indicate that LARP1 binds to HCV, an event associated with retention of intracellular infectivity.
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Dates et versions

hal-03932487 , version 1 (20-07-2023)

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Marie‐laure Plissonnier, Jessica Cottarel, Eric Piver, Majlinda Kullolli, Federica Grazia Centonze, et al.. LARP1 binding to hepatitis C virus particles is correlated with intracellular retention of viral infectivity. Virus Research, 2019, 271, pp.197679. ⟨10.1016/j.virusres.2019.197679⟩. ⟨hal-03932487⟩
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