Varicella-zoster virus envelope glycoprotein (VZV envelope glycoprotein (no universal single abbreviation; individual proteins are commonly abbreviated, e.g., gB, gH, gE))

Varicella-zoster virus envelope glycoproteins comprise at least ten distinct membrane proteins encoded by the VZV genome: gB, gH, gL, gE, gI, gK, gC, gM, gN, and ORFS/L[1][7]. These proteins orchestrate critical steps in viral attachment, entry by fusion, transport within cells, and assembly of infectious particles[1][2][3][4][7]. The core fusion machinery consists of gB (the main fusogen), gH, and gL, which facilitate membrane merger and viral entry. gE, the most abundant glycoprotein, together with gI, is central to cell-to-cell viral spread, skin tropism, and immune evasion through interactions with host proteins such as insulin-degrading enzyme[3]. Several VZV envelope glycoproteins are essential for viral replication and pathogenicity. They are prime targets for neutralizing antibodies elicited during natural infection or vaccination and are investigated as molecular targets for therapeutic interventions and diagnosis[1][4][7]. Disruption of specific glycoproteins or their domains can markedly impair viral spread, fusion, and tissue tropism, underscoring their central role in disease biology and treatment strategies[2][3][4][5][6].

Other names

VZV glycoproteinsVaricella envelope glycoproteinsViral envelope glycoproteins (specifically for VZV)

- **Neutralizing antibodies** bind glycoproteins (e.g., mAb 93k binds gB) and impede membrane fusion, preventing viral entry and spread[4]. - **Vaccines** induce host immunity, leading to the production of such neutralizing antibodies[1][4].