Epstein-Barr virus glycoprotein 350 (gp350)

Epstein-Barr virus glycoprotein 350 (gp350) is the major envelope glycoprotein of human herpesvirus 4 (EBV). It is responsible for mediating the initial attachment of the virus to the host B cells by binding to complement receptor 2 (CR2/CD21) and, to a lesser extent, CR1/CD35. gp350 exists as two main splice variants (~350 and ~220 kDa), but both variants retain the essential N-terminal domain for receptor binding. The glycan-free surface of gp350 enables specific interaction with CR2, positioning EBV for entry into B cells. This interaction is critical for EBV's host tropism and is a principal target for neutralizing antibodies and vaccine development. Antibodies that block the binding site can effectively neutralize infection in vitro and vaccine candidates based on soluble gp350 have reached clinical trials, though with mixed results for the prevention of infection. gp350 plays a key role in EBV-associated diseases, including infectious mononucleosis and multiple lymphoid malignancies, by facilitating the initial step of infection and shaping immune responses against EBV [1][3][4][5][6][9].

Other names

gp350gp350/220 (refers to splice variant)major envelope glycoprotein of EBV

Neutralization of viral entry (blocking gp350-CR2 interaction), Preventing attachment to host cells, Inhibiting virus-host receptor engagement