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Glycoprotein B (gB) is an essential envelope protein found in all herpesviruses, including human cytomegalovirus (HCMV), herpes simplex virus (HSV), and Epstein-Barr virus (EBV). As a class III viral fusion protein, gB mediates the fusion of the viral envelope with host cell membranes, a critical step for viral entry and cell-to-cell spread[1][2][6][8][9]. gB elicits strong immune responses and is a major target of neutralizing antibodies, but the majority of the antibody response is non-neutralizing due to extensive glycosylation that shields key neutralizing epitopes[1][3][4][5][8]. It also induces innate immune signaling, interacts with cellular receptors (e.g., Toll-like receptor 2, integrins), and is involved in viral maturation and egress[2][6][9]. gB has been used as a vaccine antigen (e.g., gB/MF59 in HCMV), but challenges remain due to immune evasion mechanisms. Its structure has been elucidated and reveals complex domain organization relevant for therapeutic and vaccine design[1][3][4][5][8].
Antibody-mediated neutralization of viral entry/fusion; Fusion inhibition: blocking viral fusion with host cell membranes; Interference with immune evasion through neutralizing/non-neutralizing epitope targeting
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