The entry glycoproteins of hepatitis C virus, E1E2, possess a novel regulatory mechanism in which protein disorder is harnessed to control their activity and their ability to evade antibodies.

Incompatibilities between the viral replication machinery and orthologs of the essential host factor cyclophilin A (CypA) contribute to the narrow host range of hepatitis C virus.

Interactions between viral genomes within the same cells can impact the selection of drug-resistant variants and this has been finessed by hepatitis C virus.

Integrated analysis of IFN-λ and HCV amino acid variation indicates the key role of host innate immunity in viral control.

Interferon lambda 4, a protein part of the innate immune response, drives major amino acids selection in patients chronically infected with hepatitis C virus.

Hepatitis C virus evades IRF1-dependent intrinsic antiviral immunity by exploiting cyclophilin A and its regulation of PKR.

Very frequent viral kinetics in liver transplant patients reveals that the liver is not only the source of hepatitis C virus (HCV) production, but also plays a major role in extracellular HCV clearance.

Exploiting virus-encoded ion channels as drug targets drove a multi-faceted approach to deriving potent small molecules targeting HCV p7, simultaneously providing new insights into its fundamental biology.

The hepatitis C virus IRES binds and remodels preassembled eukaryotic translation preinitiation complexes, using specific initiation factor protein within a "bacterial-like" mode of initiation that can function in both stressed and unstressed cells.

Polymorphisms in the IFNL4 gene that affect both the form and the activity of the coded protein are associated with changes in the hepatitis C virus.