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Herpes simplex virus glycoprotein D (gD) is a critical component of the HSV-1 and HSV-2 envelope, serving as the primary ligand for viral entry into host cells [UniProt P06476, P04290]. It binds to specific cellular receptors, including herpesvirus entry mediator (HVEM) and nectins, triggering a conformational change that facilitates membrane fusion in conjunction with other glycoproteins [PMID: 25653444]. As a highly immunogenic protein, gD is a primary target for the development of prophylactic and therapeutic vaccines, as well as monoclonal antibody therapies [PMID: 22219316]. While numerous gD-based vaccine candidates have demonstrated the ability to elicit strong neutralizing antibody responses, achieving consistent clinical protection against infection remains a significant challenge [PMID: 22219316]. Understanding the structural dynamics of gD and its interaction with host receptors is essential for designing more effective interventions against herpes simplex virus infections [PMID: 34161315]. Beyond its role in entry, gD is also involved in cell-to-cell spread of the virus, making it a versatile target for neutralizing agents [PMID: 25653444].
Induction of neutralizing antibodies that block viral attachment and entry into host cells by interfering with gD binding to receptors like HVEM and Nectin-1 [PMID: 25653444]. It also stimulates T-cell mediated immunity to control viral replication and spread [PMID: 28115414].
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