Glycoprotein D of herpes simplex virus 2 (gD (HSV-2))

Glycoprotein D of herpes simplex virus 2 (gD-2) is a type I transmembrane envelope glycoprotein essential for viral entry and cell-to-cell spread[1][4][5][7]. It mediates virus attachment to host cells by binding to specific entry receptors, including nectin-1, herpesvirus entry mediator (HVEM), and modified heparan sulfates[3][4][5][7]. The protein's N-terminal region binds to these host receptors, triggering a conformational change that activates the viral membrane fusion machinery through interaction with other viral glycoproteins (gH/gL and gB)[2][4][6]. Structurally, gD features a core immunoglobulin-like fold, N- and C-terminal extensions, and conserved disulfide bonds critical for its function and receptor interactions[1][4][5][7]. Antibodies that block gD or its receptor interactions have been found to inhibit infection, making gD-2 a major target for vaccine and antiviral research[6].

Other names

gD-2HSV-2 glycoprotein D

Neutralizing antibodies block receptor binding or fusion triggering. Vaccine-induced immunity elicits antibodies to prevent viral entry.