Herpes simplex virus 2 surface glycoproteins

Herpes simplex virus 2 (HSV-2) surface glycoproteins, including gB, gC, gD, and the gH/gL complex, are essential components of the viral envelope required for host cell infection (UniProt P06437). These proteins mediate a coordinated entry process involving initial attachment to heparan sulfate proteoglycans and subsequent high-affinity binding to receptors like nectin-1 or HVEM (PubMed: 24131556). Following receptor binding, the glycoproteins undergo conformational changes that trigger the fusion of the viral envelope with the host cell membrane, allowing the viral capsid to enter the cytoplasm (PubMed: 17224463). Because they are critical for infectivity and are exposed on the virion surface, these glycoproteins are primary targets for neutralizing antibodies and entry-inhibitor drugs. For instance, docosanol is a topical antiviral that is thought to inhibit the fusion of various enveloped viruses, including HSV-2, by stabilizing the host cell membrane (PubChem CID 12620). Additionally, specific monoclonal antibodies like UB-621 are designed to target gD to block viral attachment and prevent both primary infection and reactivation (PubMed: 33434155). These glycoproteins also serve as the basis for many subunit vaccine candidates aimed at eliciting a robust immune response against genital herpes. Therapeutic challenges include the high diversity of glycoproteins across different enveloped viruses and the need for agents that can effectively penetrate the site of infection.

Other names

HSV-2 envelope proteinsViral surface glycoproteinsEnveloped virus fusion proteinsgBgDgH/gL complexgCgGgEgI

Inhibition of viral entry by blocking attachment to host receptors or preventing the fusion of the viral envelope with the host cell membrane.