Epstein-Barr virus major envelope glycoprotein gp350 (gp350)

EBV glycoprotein gp350 is the principal glycoprotein found on the surface of Epstein-Barr virus particles and is highly glycosylated. It mediates the initial attachment of EBV to B cells by binding specifically to the cellular complement receptor 2 (CR2/CD21). The CR2-binding site on gp350 is a non-glycosylated surface patch, allowing specific molecular recognition despite extensive glycosylation elsewhere. This binding is an essential step for EBV to infect host cells and underlies its tropism for B cells. gp350 is targeted by potent neutralizing antibodies such as 72A1, and epitope mapping has identified dominant neutralizing regions that are the focus of vaccine development. Because gp350-mediated entry is a unique step in the EBV lifecycle and directly linked to the development of EBV-driven diseases, it remains a central focus for novel therapeutics, including antibody drugs and prophylactic vaccines.

Other names

gp350/220EBV gp350EBV envelope glycoprotein gp350

Neutralizing antibodies: block gp350 binding to the CR2 receptor, preventing viral attachment and entry. CR2-Fc analogs: act as decoys to competitively inhibit gp350 binding sites, thus neutralizing the virus. Vaccine candidates: elicit immune response targeting gp350 to prevent infection.