Epstein-Barr virus envelope glycoprotein 350 (gp350)

Epstein-Barr virus envelope glycoprotein 350 (gp350) is the major surface protein of EBV, encoded by the BLLF1 gene, and is the principal mediator of the virus’s ability to infect B lymphocytes[1][2][7]. It is a heavily glycosylated protein (~907 amino acids) that binds specifically to complement receptor type 2 (CR2, also known as CD21 or complement receptor 2) on the surface of B cells, thus facilitating viral attachment and subsequent entry[2][3][4][5][6][7]. The glycan-free region in its N-terminal domain forms the critical binding surface for CR2, and this interaction is essential for efficient infection of B cells[3][4][6]. Blocking this interaction with neutralizing antibodies or receptor mimetics prevents EBV entry, making gp350 a leading target for vaccine and therapeutic antibody development[4][6][8]. In addition to infecting B cells, gp350 plays a lesser but detectable role in infecting other cell types, such as epithelial cells, through additional mechanisms[5]. gp350 serological responses are widely used as markers for EBV infection and immunity[5]. No small-molecule inhibitors of gp350 are in clinical use, but multiple antibody-based experimental agents and vaccine strategies are in development[6][8].

Other names

Membrane antigen (MA)Envelope glycoprotein GP350gp350/220BLLF1

Blockade of gp350–CR2 interaction (by monoclonal antibodies or soluble receptor mimetics), thereby preventing EBV attachment and entry into B cells