Glycoprotein L (gL)

Glycoprotein L (gL) is an essential viral envelope protein found in all herpesviruses; it forms a tightly associated heterodimer with glycoprotein H (gH), creating the gH/gL complex that controls membrane fusion, a critical step for viral entry into host cells[5][4][8]. Unlike gH, gL lacks a transmembrane region and is necessary for the correct folding, trafficking, and function of gH; together, the complex orchestrates fusion via direct activation of glycoprotein B (gB)[5]. The gH/gL complex also mediates receptor engagement—such as binding integrins for epithelial infection—making gL a target for neutralizing antibodies and fusion-blocking interventions[4][8]. The protein is highly conserved among herpesviruses, with some species-specific differences influencing host tropism and immune targeting[4][5][8]. It is not a human receptor/enzyme, but belongs to the “viral glycoprotein—entry/fusion machinery” molecular class, and as such, is a validated target for antiviral research and mechanistic studies in viral pathogenesis.

Other names

gLHerpesvirus glycoprotein LEpstein-Barr virus glycoprotein LHSV-1/2 glycoprotein LVaricella-zoster virus glycoprotein L

Inhibition of the gH/gL/gB complex formation or function; Neutralizing antibody blockade of protein-protein interaction or conformational transition needed for fusion; Blocking interaction with cell surface receptors (e.g., integrins or others)