Herpes simplex virus glycoprotein (HSV glycoprotein)

Herpes simplex virus (HSV) glycoproteins are a group of surface proteins essential for the viral life cycle, facilitating attachment, fusion, and cell-to-cell spread (UniProt P06476, P06437). The most prominent members, such as glycoprotein D (gD), glycoprotein B (gB), and the gH/gL complex, are critical for the virus to enter host cells by interacting with receptors like nectin-1 and HVEM (PMID: 24109117). In the context of vaccine development, these glycoproteins serve as primary antigens designed to elicit both neutralizing antibodies and cellular immune responses (PMID: 32843448). By targeting these proteins, therapeutic and prophylactic vaccines aim to prevent primary infection or reduce the frequency and severity of viral reactivation in individuals with latent infections. Historically, gD has been the most widely studied antigen, though modern approaches often combine multiple glycoproteins or utilize mRNA platforms to enhance immunogenicity (Moderna, 2024; BioNTech, 2024). These antigens are pivotal in addressing diseases caused by HSV-1 and HSV-2, ranging from common oral and genital lesions to severe conditions like neonatal herpes and viral encephalitis (PMID: 33619384).

Other names

HSV envelope glycoproteinHerpes simplex virus type 1 glycoproteinHerpes simplex virus type 2 glycoproteingDgBgCgH/gL complex

Vaccines targeting these glycoproteins induce the production of neutralizing antibodies that bind to the viral envelope, preventing the virus from attaching to and fusing with host cell membranes (PMID: 24109117). Additionally, these antigens stimulate T-cell mediated immunity, specifically CD4+ and CD8+ cells, which help recognize and eliminate HSV-infected cells and control viral latency (PMID: 32843448).