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Epstein-Barr virus glycoprotein B (gB) is the most conserved envelope glycoprotein among herpesviruses and forms homotrimers that act as the core fusion protein, mediating the essential step of combining the viral envelope with the host cell membrane to allow viral entry. gB is indispensable for viral maturation, egress, and infection of both B cells and epithelial cells. Its structure consists of several domains with substantial post-translational modifications (like glycosylation), and undergoes major conformational changes during fusion. Neutralizing antibodies directed against gB domains can block infection, highlighting its role as a promising target for vaccine and antiviral strategies. Because EBV infection is implicated in several human cancers and lifelong persistence, gB’s function is integral to the underlying pathophysiology of both acute and latent EBV-related diseases.
Inhibition of membrane fusion (by blocking gB activation or conformational change) Prevention of viral entry and replication (antibodies that neutralize gB prevent infection in vitro)
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