Herpes simplex virus 1 envelope glycoproteins (HSV-1 glycoproteins)

Herpes simplex virus 1 (HSV-1) envelope glycoproteins are a complex group of proteins, including gB, gC, gD, gH, and gL, that are essential for the virus's ability to infect host cells. These proteins are embedded in the viral lipid envelope and coordinate the multi-step process of viral entry, which involves initial attachment to cell surface heparan sulfate, high-affinity binding to specific entry receptors like nectin-1 or HVEM, and subsequent fusion of the viral envelope with the host cell membrane (UniProt, 2023). Glycoprotein D (gD) is the primary receptor-binding protein, while the gH/gL complex and gB function as the core fusion machinery (PubMed: 23536660). In the context of disease, these glycoproteins are critical for the establishment of primary infection and the subsequent spread of the virus during periodic reactivations, leading to conditions ranging from common cold sores to life-threatening encephalitis (StatPearls, 2023). Because they are exposed on the surface of the virion, they are the primary targets for neutralizing antibodies and are the focus of vaccine development and entry-inhibitor therapies. Drugs like docosanol interfere with the fusion process mediated by these proteins, while experimental monoclonal antibodies like UB-621 target specific glycoproteins to block viral entry and cell-to-cell transmission (NIH, 2022).

Other names

HSV-1 surface proteinsHSV-1 envelope proteinsGlycoprotein B (gB)Glycoprotein C (gC)Glycoprotein D (gD)Glycoprotein H (gH)Glycoprotein L (gL)Glycoprotein G (gG)

Inhibition of viral-host cell membrane fusion, neutralization of viral particles by blocking receptor binding, and prevention of viral attachment to host cell surface glycosaminoglycans.