Proteomics of HCV virions reveals an essential role for the nucleoporin Nup98 in virus morphogenesis.

ABSTRACT: Hepatitis C virus (HCV) is a unique enveloped virus that assembles as a hybrid lipoviral particle by tightly interacting with host lipoproteins. As a result, HCV virions display a characteristic low buoyant density and a deceiving coat, with host-derived apolipoproteins masking viral epitopes. We previously described methods to produce high-titer preparations of HCV particles with tagged envelope glycoproteins that enabled ultrastructural analysis of affinity-purified virions. Here, we performed proteomics studies of HCV isolated from culture media of infected hepatoma cells to define viral and host-encoded proteins associated with mature virions. Using two different affinity purification protocols, we detected four viral and 46 human cellular proteins specifically copurifying with extrace

SUBMITTER: Lussignol M 

PROVIDER: S-EPMC4780614 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature