Hepatitis C virus envelope glycoprotein E1 (E1)

Hepatitis C virus envelope glycoprotein E1 is a type I transmembrane protein that, together with E2, forms the viral envelope glycoprotein complex essential for HCV entry into host hepatocytes[1][2][3][6][7]. E1 (192 amino acids) consists of a highly glycosylated N-terminal ectodomain and a C-terminal transmembrane domain, and engages in non-covalent heterodimerization with E2[1][2][7]. It is believed to act as the *fusogenic* subunit, mediating viral membrane fusion with the host[2][4][6]. E1 is a major antigenic component of the HCV virion surface, triggering neutralizing antibody responses[3][4]. The E1/E2 complex plays a critical role in viral infectivity, immune evasion, and is the primary target for neutralizing antibodies and candidate vaccines[4][6]. High structural variability and dense glycosylation present significant barriers to drug and vaccine design[4][6].

Other names

E1 glycoproteinHCV envelope protein E1HCV E1

Inhibition of viral entry/fusion by blocking E1/E2 complex function (by neutralizing antibodies or experimental inhibitors)[4][6]