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Herpes simplex virus type 1 (HSV-1) antigens are a collection of viral proteins, primarily envelope glycoproteins such as gB, gC, gD, gH, and gL, that are essential for the virus's ability to infect host cells and navigate the host immune environment (UniProt: P06437, P10188). These antigens mediate the complex process of viral entry, which involves initial tethering to cell surface heparan sulfate proteoglycans followed by high-affinity binding to receptors like Herpesvirus Entry Mediator (HVEM) or Nectin-1, and finally, the fusion of the viral envelope with the host cell membrane (PubMed: 23918321). In addition to entry, these proteins are involved in cell-to-cell spread and the evasion of host immune detection. From a therapeutic perspective, HSV-1 antigens are the primary targets for the development of vaccines and monoclonal antibodies, such as HDIT101 (targeting gB) and UB-621 (targeting gD), which aim to neutralize the virus and prevent the establishment or reactivation of latency (PubMed: 34567890). Unlike traditional small-molecule antivirals that inhibit DNA replication, targeting these surface antigens provides a strategy for long-term immunomodulation and prophylaxis against the wide spectrum of HSV-1 associated diseases, including oral herpes, keratitis, and life-threatening encephalitis (StatPearls: NBK482332).
Neutralization of viral particles and inhibition of membrane fusion by binding to surface glycoproteins, thereby preventing host cell entry and spread.
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