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Epstein–Barr virus envelope glycoprotein B (gB) is a large (approximately 857 amino acids) membrane protein located in the viral envelope. It executes membrane fusion during EBV entry into epithelial cells and B cells: after EBV glycoprotein binding to cell surface receptors, gB undergoes conformational changes that mediate fusion of viral and cellular membranes, allowing viral genome entry. The protein is essential for viral infectivity, and its expression levels significantly influence EBV’s ability to infect cells. gB has three main domains: an ectodomain (with extensive glycosylation), a transmembrane domain, and a cytoplasmic tail. In cell entry: - For B cells, EBV engages CR2 (CD21) via gp350, triggers gB fusion after gp42 binds MHC II. - For epithelial cells, gB is activated following engagement of cellular integrins (αvβ6/αvβ8) by gH/gL. gB is a canonical antiviral target, but currently there are no clinically approved molecules specifically targeting gB for EBV infection. Inhibiting gB-mediated fusion is an active area of drug and vaccine research to prevent or treat EBV-associated diseases.
Entry inhibition (drugs/antibodies that prevent fusion or gB activation block virus entry into cells)
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