Envelope glycoprotein E of varicella-zoster virus (gE)

Envelope glycoprotein E (gE) of varicella-zoster virus is the most abundant glycoprotein in the viral envelope and is essential for VZV replication, assembly, and mediation of cell-to-cell transmission[6][1][5]. It is translated from the VZV ORF68 gene product and forms a heterodimer with glycoprotein I (gI), an interaction necessary for efficient trafficking, maturation, and cell-to-cell spread[1][3][5]. gE binds the insulin-degrading enzyme (IDE) on host cells, which acts as a proposed cellular receptor, facilitating viral entry. The N-terminal region of gE is uniquely required for VZV replication, cell tropism (notably for skin and T cells), and for interactions with IDE and gI[1][5]. gE is highly immunogenic, containing antigenic epitopes critical for the host neutralizing antibody response and forms the basis of most VZV vaccines (e.g., varicella and recombinant zoster vaccines)[6]. Its functions include roles in attachment, membrane fusion, replication, and immune evasion, making it a validated therapeutic target that is essential for the VZV life cycle and pathogenesis[1][5][6][7].

Other names

Glycoprotein EgEVZV gEORF68 protein

Vaccine-induced neutralizing antibodies target gE, blocking attachment and cell entry; Vaccine-generated T-cell response targets gE-expressing infected cells; Immunological blockade of cell-to-cell viral spread.