Glycoprotein D of herpes simplex virus (gD)

Glycoprotein D (gD) is an essential envelope glycoprotein present on the surface of herpes simplex virus (HSV) types 1 and 2, required for viral infectivity and entry into host cells[1][6][7]. gD acts by binding to multiple host cell receptors including nectin-1, herpesvirus entry mediator (HVEM, TNFRSF14), and 3-O-sulfated heparan sulfate, thereby determining the tropism of HSV and facilitating viral fusion with the cell membrane[2][3][4][7]. Binding of gD to a cellular receptor triggers conformational changes that activate other viral glycoproteins (gH/gL and gB), resulting in fusion of the viral and cellular membranes for virus entry[3][4][5]. gD is also a major antigenic target in vaccine development against HSV and in diagnostic assays; neutralizing antibodies against gD can block viral entry and fusion, representing an important antiviral strategy[5]. Structural studies indicate that gD consists of regions responsible for receptor binding and fusion activation, with antigenic and structural differences between HSV-1 and HSV-2 gD variants[1][6].

Other names

Glycoprotein DgDHSV-1 gDHSV-2 gDEnvelope glycoprotein D

Blocking gD-receptor interactions to prevent virus entry Neutralizing antibody binding to gD to inhibit infection/fusion