Herpes simplex virus type 2 glycoprotein L (gL)

Herpes simplex virus type 2 (HSV-2) glycoprotein L (gL) is an essential component of the viral entry and fusion machinery (UniProt P28278). It forms a stable heterodimeric complex with glycoprotein H (gH), which is required for the fusion of the viral envelope with the host cell membrane during infection (PubMed: 24942591). Beyond its structural role, gL acts as a molecular chaperone, ensuring the proper folding, processing, and intracellular trafficking of gH to the virion surface (UniProt P28278). The gH/gL complex is a primary target for the host's neutralizing antibody response and is a key focus in the development of next-generation prophylactic and therapeutic vaccines (NIH: PMC7540718). While no drugs specifically targeting gL are currently approved, it remains a high-priority target for subunit and mRNA-based vaccines aimed at preventing viral entry and reducing the severity of genital herpes (J. Virol. 1997;71:2940-2946). Experimental monoclonal antibodies, such as LP11, have demonstrated the potential to neutralize the virus by blocking the gH/gL-gB interaction (MDPI: Viruses 2020, 12, 1045).

Other names

UL1 proteinEnvelope glycoprotein LgL-2HHV-2 gL

Inhibition of viral entry and membrane fusion through neutralization of the gH/gL complex.