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Herpes simplex virus (HSV) surface glycoproteins are a group of essential proteins embedded in the viral envelope that mediate the complex process of viral entry into host cells. The core entry machinery consists of four primary glycoproteins: gD, which serves as the receptor-binding protein; gB, the primary fusogen; and the gH/gL heterodimer, which regulates gB activity (Campadelli-Fiume et al., 2007, Reviews in Medical Virology). Other glycoproteins like gC facilitate initial attachment to heparan sulfate proteoglycans, while gE/gI complexes are involved in cell-to-cell spread and immune evasion (NIH/NIAID). These proteins are critical for the pathogenesis of HSV-1 and HSV-2, which cause conditions ranging from oral and genital herpes to life-threatening encephalitis and neonatal infections (StatPearls). Because these glycoproteins are exposed on the surface of the virion and infected cells, they are prime targets for neutralizing antibodies and entry inhibitors. For example, Docosanol is an FDA-approved topical agent that is thought to inhibit the fusion between the viral envelope and the host cell membrane (PubChem). Newer therapeutic candidates, such as the monoclonal antibodies UB-621 (targeting gD) and HDIT101 (targeting gG-2), are being investigated for their ability to reduce viral shedding and provide passive immunity (ClinicalTrials.gov). This class of targets is particularly valuable for developing therapies that can prevent initial infection or limit the spread of the virus in patients who are resistant to standard nucleoside analogs.
Inhibition of viral attachment to host cell receptors, prevention of membrane fusion between the viral envelope and host cell plasma membrane, and neutralization of extracellular virions (PubMed).
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