Herpes simplex virus 2 glycoprotein B (gB) (HSV-2 gB)

Herpes simplex virus 2 glycoprotein B (HSV-2 gB) is a highly conserved class III viral fusion protein that is essential for the entry of the virus into host cells [2, 3]. It exists as a homotrimeric spike on the viral envelope and functions as the core fusogen, working in tandem with glycoproteins gD and the gH/gL complex to facilitate the merger of the viral envelope with the host cell plasma or endosomal membrane [13, 16]. Beyond its primary role in membrane fusion, gB is involved in initial viral attachment by binding to heparan sulfate proteoglycans and interacts with specific host cell receptors such as PILR-alpha [8, 10]. As a major target for the host immune system, gB is a primary focus for the development of neutralizing monoclonal antibodies and subunit vaccines designed to prevent or treat genital and neonatal herpes [6, 18]. Therapeutic agents targeting gB, such as the monoclonal antibody HDIT101, aim to neutralize the virus by blocking its ability to undergo the extensive conformational rearrangements required for fusion, thereby preventing the delivery of the viral genome into the host cytoplasm [1, 6]. Additionally, gB plays a critical role in the cell-to-cell spread of the virus, making it a vital target for controlling chronic and recurrent infections [5, 11].

Other names

Envelope glycoprotein BgB2UL27Human herpesvirus 2 glycoprotein B

Neutralization of viral entry by blocking the conformational change from prefusion to postfusion states, inhibition of membrane fusion between the viral envelope and host cell membrane, and prevention of cell-to-cell viral spread.