Herpes simplex virus 2 glycoprotein D (gD)

Herpes simplex virus 2 glycoprotein D (HSV-2 gD) is a viral envelope glycoprotein essential for HSV-2 entry into host cells. It binds to cell surface receptors such as nectin-1 (primarily in neurons and epithelial cells), nectin-2, and HVEM (TNFRSF14), initiating a conformational change that triggers membrane fusion mediated by viral glycoproteins gB and gH/gL.[1][2][3][9] The protein features an IgV-like core domain flanked by flexible N- and C-terminal extensions; receptor binding displaces these extensions, exposing fusion machinery.[1][3] Crystal structures show HSV-2 gD engages nectin-1 via distinct sites compared to HVEM, yet induces similar activation, with key interactions involving residues like Arg222 on gD and Phe129/Glu125 on nectin-1.[1][3] This conserved mechanism across HSV-1 and HSV-2 underscores gD's role in broad cell tropism.[3][9] As a key viral component, gD is a prime antiviral target, though no approved drugs directly interact with it; therapeutic strategies focus on blocking receptor binding to prevent infection.[1][2][9]

Other names

HSV-2 gDenvelope glycoprotein D