Hepatitis C virus E1 envelope glycoprotein (HCV E1)

The Hepatitis C virus (HCV) E1 envelope glycoprotein is a critical structural protein required for viral entry and fusion with host cell membranes [PubMed: 24501412]. It is a type I transmembrane protein that forms a non-covalent heterodimer with the E2 glycoprotein on the surface of the virion [UniProt: P26664]. While E2 is the primary receptor-binding protein, E1 is thought to facilitate the pH-dependent fusion of the viral envelope with the endosomal membrane, allowing the viral genome to enter the host cell cytoplasm [PubMed: 15140980]. E1 is essential for the pathogenicity of HCV, which causes chronic liver infection, cirrhosis, and hepatocellular carcinoma [PubMed: 30551056]. Although current direct-acting antivirals (DAAs) primarily target non-structural proteins, E1 is a major focus for the development of prophylactic vaccines and entry inhibitors [PubMed: 28250128]. Therapeutic challenges include the protein's high genetic variability and extensive N-linked glycosylation, which masks critical epitopes from the host immune system [PubMed: 17222464].

Other names

E1Envelope glycoprotein E1gp35HCV E1 protein

Neutralization of viral particles and blockade of the E1-mediated membrane fusion process during viral entry [PubMed: 24501412].