Varicella-zoster virus envelope glycoprotein E (gE (VZV gE))

Varicella-zoster virus envelope glycoprotein E (gE) is the most abundant and immunodominant surface glycoprotein encoded by VZV, an alpha-herpesvirus responsible for varicella (chickenpox) and herpes zoster (shingles). gE is a type I transmembrane protein with a unique ~188 amino acid N-terminal region essential for VZV replication, secondary envelopment, and efficient spread both in vitro and in skin and T cells in vivo. gE forms non-covalent heterodimers with glycoprotein I (gI), a complex critical for trafficking, virion morphogenesis, and cell-cell spread. gE also interacts with the insulin-degrading enzyme (IDE), which modulates VZV infectivity and cell entry, although IDE is not strictly required for neuronal infection. The gE/gI complex facilitates viral pathogenesis by contributing to cell-to-cell contacts and possibly by modulating host tight junctions and cytoskeletal elements. Recombinant VZV gE is the antigen used in the Shingrix vaccine, which induces strong humoral and cellular immunity, providing protection against reactivation of VZV. Disruption or mutation of the gE gene severely impairs VZV replication, confirming its essential role in the viral life cycle.

Other names

Glycoprotein EgEVZV gEVZV envelope glycoprotein E

Vaccination (e.g., Shingrix) elicits antibody and cellular immune responses against gE, blocking virus spread and promoting immune-mediated clearance. Neutralizing antibodies can bind gE to prevent cell entry and fusion. Antibody-based detection is used in serological assays.