Epstein–Barr virus envelope glycoprotein

Epstein–Barr virus envelope glycoproteins are viral surface proteins essential for EBV’s infection of human B cells and epithelial cells[6][8]. The major glycoproteins include gp350, which mediates attachment to CD21 (CR2) on B cells[3][4][5], and the core fusion machinery, composed of glycoprotein B (gB), glycoprotein H (gH), and glycoprotein L (gL), which enable fusion of the viral envelope with the host cell membrane during entry[1][2][6][7]. gp42 is also part of a tripartite complex active during B cell infection, interacting with HLA class II to facilitate membrane fusion[6][8]. These glycoproteins are considered important therapeutic and vaccine targets—for example, gp350 is the leading antigen for prophylactic vaccine development[6]. Their roles also extend to immune evasion, as some (e.g., BILF1, BARF1) downregulate host immune responses[6]. Their expression is critical in EBV-mediated oncogenesis, especially in certain lymphomas and nasopharyngeal carcinoma[3][6][8]. Blocking these glycoproteins can prevent EBV entry into cells, making them a focal point for antiviral strategies and vaccine efforts.

Other names

gp350gp220 (splicing isoform of gp350)glycoprotein B (gB)glycoprotein H (gH)glycoprotein L (gL)gp42BMRF2BILF1BARF1 (all are envelope glycoproteins encoded by EBV)

Inhibition of virus-host cell fusion (by blocking glycoprotein–receptor interaction); Blocking of viral attachment to host cells