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.

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

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

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

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.

A conformational change in the Cricket Paralysis Virus IRES upon double translocation in the ribosome uncovers an unexpected similarity with the Hepatitis C Virus IRES.

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.

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.

Naïve CD8⁺ T cells are dysregulated during chronic hepatitis C (HCV) infection, and this is reversible after viral clearance.