Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly.
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Interestingly, however, at three distinct regions the chemical shifts in solution differ significantly between core proteins in the capsid state versus in the dimer state,
However, early studies of cells infected with the JFH-1 virus showed that the core protein was detected at the surface of lipid droplets or in association with the ER membranes
25-27 Although this cellular model is based on HCV core protein production from a genotype 1a virus, it also displays the accumulation and clustering of lipid droplets
For cells expressing wild-type HBc (Fig. 5G; yellow dots), most of the measurements showed that this protein was essentially in an oligomeric form, and this even at low protein
This phenomenon was observed in the hepatoma cell line Huh7 infected with the complete virus (the JFH-1 strain), but also in Huh7 cells producing only the mature HCV core
Moreover, an absence of core protein at the LD sur- face was associated with higher levels of virus secretion for the C10M-JFH-1 construct than for the wt-JFH-1 construct,
Altogether, these results demonstrated that the domi- nant negative property of GagG110V mainly relies on nuclear retention of wild-type Gag, precluding Gag nuclear export
Core protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membrane.: HCV core protein domain involved in viral