Epstein-Barr virus glycoproteins gp350, gH, gL, and gB (EBV gp350/gH/gL/gB)

The Epstein-Barr virus (EBV) glycoproteins gp350, gH, gL, and gB constitute the core machinery required for the virus to attach to and enter host cells, specifically B lymphocytes and epithelial cells [2, 15]. Gp350 (encoded by BLLF1) is the most abundant envelope protein and mediates initial attachment to the host cell receptor CD21 (CR2) [17, 20]. The gH/gL heterodimer (encoded by BKRF2 and BLRF1) acts as a regulator of membrane fusion, while gB (encoded by BALF4) serves as the primary viral fusogen that merges the viral envelope with the host cell membrane [12, 18, 23]. These proteins are critical therapeutic targets because neutralizing antibodies against them can block viral entry and prevent primary infection or reactivation [1, 3]. Current drug development efforts include mRNA-based vaccines, such as mRNA-1189, and monoclonal antibodies like AMMO1, which are designed to elicit or provide broad protection against EBV-associated diseases including infectious mononucleosis, various lymphomas, and multiple sclerosis [5, 7, 10].

Other names

EBV envelope glycoproteinsEBV entry machinerygp350/220gH/gL complexGlycoprotein BBLLF1 (gp350)BKRF2 (gH)BLRF1 (gL)BALF4 (gB)

Neutralization of viral entry by inhibiting attachment to host receptors (e.g., CD21 via gp350) and blocking the membrane fusion machinery (gH/gL and gB) required for viral penetration into B cells and epithelial cells.