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Epstein-Barr virus (EBV) envelope glycoprotein B (gB) is a highly conserved class III viral fusion protein that is essential for the virus to enter host cells. It serves as the core fusogen, executing the fusion of the viral envelope with the host cell membrane—including both B cells and epithelial cells—after being triggered by the gH/gL complex [1, 3, 14]. EBV gB is a primary target for the development of prophylactic and therapeutic interventions, as neutralizing antibodies against gB can block viral infection and potentially prevent associated diseases such as infectious mononucleosis, Burkitt lymphoma, and nasopharyngeal carcinoma [2, 3, 60]. Recent clinical research has also strongly linked EBV infection to the development of multiple sclerosis, further elevating the importance of gB as a vaccine and drug target [12, 19, 34]. Several experimental monoclonal antibodies, such as AMMO5 and 3A3, and multivalent mRNA vaccines like Moderna's mRNA-1194 are currently under investigation for their ability to target gB and provide broad protection against EBV-related pathologies [27, 36, 60].
Inhibition of viral-cell membrane fusion and neutralization of viral entry into host B cells and epithelial cells.
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