Herpes simplex virus type 2 surface glycoproteins (HSV-2 glycoproteins)

Herpes simplex virus type 2 (HSV-2) surface glycoproteins, primarily gB, gC, gD, gH, and gL, are essential mediators of viral entry into host cells (Agelidis & Shukla, 2015, PMID: 25681707). These proteins function in a coordinated cascade where gC and gB initiate attachment by binding to cell-surface heparan sulfate proteoglycans (UniProt Consortium, 2024). Subsequently, gD binds to specific entry receptors such as Nectin-1 and Herpesvirus Entry Mediator (HVEM), which triggers a conformational change in the gH/gL complex (Carfi et al., 2001, PMID: 11533492). This activation allows the fusion protein gB to merge the viral envelope with the host cell membrane, facilitating capsid release into the cytoplasm (Heldwein & Krummenacher, 2008, PMID: 18587440). As the primary interface between the virus and the host, these glycoproteins are the principal targets for neutralizing antibodies and are the focus of subunit vaccine development and entry-inhibitor therapeutics (United BioPharma, 2023). Blocking these interfaces aims to prevent the initial infection of epithelial cells and the subsequent establishment of latency in sensory neurons (Heidelberg ImmunoTherapeutics, 2022).

Other names

Herpes simplex virus type 2 envelope glycoproteinsHSV-2 entry proteinsgB/gC/gD/gH/gL complexHSV-2 attachment proteinsGlycoprotein B (gB)Glycoprotein C (gC)Glycoprotein D (gD)Glycoprotein H (gH)Glycoprotein L (gL)

Inhibition of viral attachment to host cell receptors (e.g., heparan sulfate, Nectin-1, HVEM) and blockade of the viral-host membrane fusion process (Agelidis & Shukla, 2015, PMID: 25681707).