LARP1 binding to hepatitis C virus particles is correlated with intracellular retention of viral infectivity.
HCV
Infectivity
LARP1
Virions
Journal
Virus research
ISSN: 1872-7492
Titre abrégé: Virus Res
Pays: Netherlands
ID NLM: 8410979
Informations de publication
Date de publication:
02 10 2019
02 10 2019
Historique:
received:
03
07
2019
accepted:
27
07
2019
pubmed:
10
8
2019
medline:
1
7
2020
entrez:
10
8
2019
Statut:
ppublish
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.
Identifiants
pubmed: 31398365
pii: S0168-1702(19)30456-3
doi: 10.1016/j.virusres.2019.197679
pii:
doi:
Substances chimiques
Autoantigens
0
Ribonucleoproteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
197679Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.