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Envelope glycoprotein GP350 is the most abundant surface protein on the Epstein-Barr virus (EBV) virion and is essential for the infection of B lymphocytes. It mediates the initial attachment of the virus to the host cell by binding to the complement receptor type 2 (CR2/CD21) or complement receptor type 1 (CD35). Due to its critical role in viral entry and its high density on the viral envelope, gp350 is the primary target for neutralizing antibodies and the most widely studied candidate for prophylactic EBV vaccines. In clinical trials, gp350-based vaccines have demonstrated the ability to significantly reduce the incidence of infectious mononucleosis, although they have historically faced challenges in completely preventing primary EBV infection. Beyond its role in acute infection, gp350 is a key target in efforts to prevent EBV-associated malignancies, such as Burkitt lymphoma and nasopharyngeal carcinoma, and is increasingly investigated in the context of EBV-linked autoimmune diseases like multiple sclerosis. Therapeutic strategies targeting gp350 include nanoparticle-based vaccines and monoclonal antibodies designed to block B-cell tethering and induce protective immunity.
Inhibition of viral attachment to B-lymphocytes by blocking the interaction between the viral gp350 protein and the host receptor CD21 (CR2), and induction of neutralizing antibodies and antibody-dependent cellular cytotoxicity (ADCC).
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