Herpes simplex virus 2 glycoprotein L (gL)

Herpes simplex virus 2 glycoprotein L (gL) is an essential viral envelope protein that forms a stable heterodimer with glycoprotein H (gH) [1, 22]. This gH/gL complex is a critical component of the core fusion machinery, alongside glycoproteins B (gB) and D (gD), which mediates the entry of HSV-2 into host cells by facilitating the fusion of the viral envelope with the host cell membrane [1, 2, 3]. Beyond its direct role in fusion, gL serves as a vital molecular chaperone required for the proper folding, maturation, and intracellular trafficking of gH; in the absence of gL, gH is retained in the endoplasmic reticulum and fails to reach the virion surface [10, 22]. Because the gH/gL complex is indispensable for infectivity and is a primary target for neutralizing antibodies, it is a focal point for the development of novel vaccines and therapeutic monoclonal antibodies [1, 2]. Targeting gL aims to block the initial stages of infection and reduce the frequency of viral reactivation and shedding in patients with genital herpes [14, 20]. While most current clinical vaccine candidates focus on other glycoproteins like gD or gB, gL remains a key target in multi-antigen strategies and antibody-based therapies due to its essential role in the viral life cycle [1, 16].

Other names

Envelope glycoprotein LUL1 proteingL2UL1 gene product

Inhibition of viral entry and membrane fusion by blocking the gH/gL complex interaction with host cell membranes or other viral glycoproteins.