Herpes simplex virus type 2 glycoprotein B (gB)

Herpes simplex virus type 2 glycoprotein B (gB) is a highly conserved, essential viral envelope protein that serves as a Class III membrane fusion protein (3, 8). It plays a dual role in the viral life cycle, mediating the initial attachment of the virus to host cell heparan sulfate proteoglycans and subsequently driving the fusion of the viral envelope with the host cell membrane in coordination with the gD and gH/gL complex (1, 4, 11). Because gB is indispensable for viral entry and cell-to-cell spread, it is a primary target for the development of neutralizing monoclonal antibodies and both prophylactic and therapeutic vaccines (5, 6). Current therapeutic strategies, such as the monoclonal antibodies HDIT101 and UB-621, aim to block viral entry or leverage Fc-mediated effector functions to control infection (12, 19). Recent research emphasizes the importance of targeting the prefusion conformation of gB to achieve more potent neutralization and prevent the establishment of latency (19, 20).

Other names

Envelope glycoprotein BgB2UL27Postfusion glycoprotein BHSV-2 gB

Neutralization of viral entry and inhibition of membrane fusion by binding to the glycoprotein B ectodomain, often requiring Fc-mediated effector functions such as antibody-dependent cellular cytotoxicity (ADCC) for optimal protection.