Hepatitis C virus E2 envelope glycoprotein (HCV E2)

Hepatitis C virus E2 envelope glycoprotein is a viral surface protein integral to the assembly of the infectious HCV particle and the entry process into host cells. E2 is a type I transmembrane glycoprotein that, together with E1, forms a heterodimer embedded in the viral lipid envelope. E2 is directly responsible for binding to essential cellular entry receptors, most notably CD81, facilitating virus fusion and ingress into hepatocytes. It is a primary target of neutralizing antibodies and is highly immunogenic, although the immune response is often subverted by the protein's marked sequence variability and glycan shielding. Structural studies reveal the E2 core domain adopts a compact, globular fold with a central immunoglobulin-like β-sandwich flanked by protein layers, departing from predictions of a typical class II fusion protein structure. E2's critical role in infection and its recognition by the immune system make it a central focus of therapeutic antibody and vaccine development efforts for hepatitis C[1][4][5][6][7].

Other names

E2 glycoproteinHCV E2 proteinEnvelope protein E2

Inhibition of virus-host cell attachment (blocking E2-CD81 binding) Viral neutralization by antibody binding