Hepatitis C virus envelope glycoprotein 1 (HCV E1)

The Hepatitis C virus envelope glycoprotein 1 (E1) is a critical structural component of the HCV virion, primarily responsible for mediating viral entry and membrane fusion into host hepatocytes (UniProt P26664). E1 is a type I transmembrane protein that forms a non-covalent heterodimer with the E2 glycoprotein, which serves as the functional unit for viral attachment and entry (PubMed: 24553139). While E2 is the main receptor-binding protein, E1 is believed to facilitate the fusion of the viral envelope with the host cell's endosomal membrane under acidic conditions (PubMed: 30108114). In the pathogenesis of Hepatitis C, E1 plays a vital role in viral assembly and the establishment of chronic infection by evading the host immune system through high genetic variability and glycan shielding (NIH: PMC4153115). Although most current direct-acting antivirals (DAAs) target non-structural proteins, E1 remains a major target for prophylactic vaccine candidates and the development of broad-spectrum neutralizing antibodies (PubMed: 22238253). Challenges in targeting E1 include its complex folding requirements and the rapid emergence of escape mutants within the viral quasispecies (PubMed: 18455118).

Other names

E1 proteinEnvelope glycoprotein 1gp35HCV E1

Neutralization of viral particles, inhibition of viral attachment to host cells, and blockade of membrane fusion.