Envelope glycoprotein L (Herpes simplex virus type 2) (gL)

Herpes simplex virus type 2 (HSV-2) glycoprotein L (gL) is an essential viral envelope protein that forms a functional heterodimer with glycoprotein H (gH) [1, 13]. This gH/gL complex is a core component of the herpesvirus entry machinery, acting as a regulator that triggers membrane fusion between the viral envelope and the host cell membrane [1, 10]. Glycoprotein L is strictly required for the correct folding, intracellular transport, and surface expression of gH; without gL, gH remains sequestered in the endoplasmic reticulum and the virus is non-infectious [1, 13]. During the entry process, the gH/gL complex interacts with other viral proteins, such as glycoprotein D (gD) and the fusogen glycoprotein B (gB), to coordinate the fusion event [7, 13]. Because of its indispensable role in viral infectivity and its accessibility on the virion surface, gL is a primary target for the development of neutralizing antibodies and novel entry inhibitors [2, 7]. While current therapies like acyclovir target viral DNA replication, targeting gL offers a strategy to block the initial infection and prevent the establishment of latency [5, 12].

Other names

gLUL1Glycoprotein LEnvelope glycoprotein L

Inhibition of viral entry and membrane fusion by blocking the formation or activity of the gH/gL complex, thereby preventing the virus from infecting host cells and spreading between cells.