Herpes simplex virus glycoprotein D (gD) (gD)

Herpes simplex virus glycoprotein D (gD) is a critical component of the HSV-1 and HSV-2 envelope, serving as the primary receptor-binding protein required for viral entry into host cells (UniProt P06476). It functions by interacting with specific host cell surface receptors, including Herpesvirus Entry Mediator (HVEM), Nectin-1, and 3-O-sulfated heparan sulfate (PubMed: 11518955). Upon binding, gD undergoes a conformational change that triggers the viral fusion machinery, consisting of glycoproteins gB and the gH/gL complex, to facilitate the merging of the viral envelope with the host cell membrane (PubMed: 21613584). Because of its essential role in the initial stages of infection, gD is a major target for the development of neutralizing antibodies, entry inhibitors, and prophylactic or therapeutic vaccines (PubMed: 24109229). Therapeutic strategies often focus on blocking the gD-receptor interface to prevent viral attachment and subsequent spread. Clinical candidates like HDIT101 and UB-621 are monoclonal antibodies designed to neutralize the virus by targeting gD, aiming to reduce viral shedding and lesion frequency in infected individuals (ClinicalTrials.gov NCT03655548).

Other names

HSV gDEnvelope glycoprotein DUS6Herpesvirus entry mediator ligandgD-1gD-2

Neutralization of viral entry by blocking the interaction between viral glycoprotein D and host receptors such as HVEM and Nectin-1.