Herpes simplex virus 2 envelope glycoproteins (HSV-2 glycoproteins)

The Herpes simplex virus 2 (HSV-2) envelope glycoproteins, primarily gB, gC, gD, and the gH/gL complex, are essential components of the viral entry machinery [13, 20]. Glycoprotein D (gD) serves as the primary receptor-binding protein, interacting with host cell receptors such as nectin-1, herpesvirus entry mediator (HVEM), and 3-O-sulfated heparan sulfate to trigger the entry process [17, 25]. Glycoprotein C (gC) and gB facilitate initial attachment to cell surface heparan sulfate proteoglycans [22, 27]. Following receptor binding by gD, a conformational signal is transmitted through the gH/gL heterodimer to activate gB, which acts as the class III viral fusogen to merge the viral envelope with the host cell membrane [19, 28]. These glycoproteins are critical for the pathogenesis of genital herpes, neonatal herpes, and the facilitation of HIV co-infection [4, 6]. Because they are exposed on the virion surface and infected cells, they are primary targets for neutralizing antibodies and vaccine development [1, 15]. Therapeutic monoclonal antibodies such as UB-621 (targeting gD) and HDIT101 (targeting gB) are currently in clinical trials to reduce viral shedding and recurrence rates in patients with chronic HSV-2 infection [2, 7]. Additionally, these proteins play roles in immune evasion, such as gC binding to complement component C3b to inhibit the host's immune response [30, 32]. Targeting these glycoproteins offers a strategy to block both initial infection and the cell-to-cell spread of the virus [11, 12].

Other names

HSV-2 entry glycoproteinsHSV-2 surface glycoproteinsHSV-2 glycoprotein B (gB)HSV-2 glycoprotein C (gC)HSV-2 glycoprotein D (gD)HSV-2 glycoprotein H (gH)HSV-2 glycoprotein L (gL)

Inhibition of viral entry by blocking host receptor binding, neutralizing viral particles, and preventing membrane fusion or cell-to-cell spread.