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Epstein–Barr virus glycoprotein gp350 is the major surface protein of EBV and plays a key role in viral entry by binding to the host B cell receptor CR2 (CD21), initiating attachment and facilitating infection[1][4][8]. The protein is highly glycosylated, with a structure that shields most surfaces except for the receptor-binding site, which is essential for host cell recognition[4]. Structural studies confirm that glycosylation is not crucial for CR2 binding but contributes to the antigenicity and stability of gp350[4][3]. Inhibition of the gp350–CR2 interaction by monoclonal antibodies or engineered CR2 analogs shows promise as a potential antiviral approach[1]. Because gp350 facilitates EBV entry into B cells, it serves as a prime target for vaccine and therapeutic antibody development to prevent EBV-associated diseases, including certain cancers and autoimmune disorders[1][4][8].
Inhibition of viral attachment by blocking gp350–CR2 interaction; Neutralizing viral infectivity by antibody binding to receptor-binding site
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