Epstein-Barr virus envelope glycoproteins involved in viral entry (EBV entry glycoproteins)

The Epstein-Barr virus (EBV) envelope glycoproteins involved in viral entry constitute a complex machinery essential for the virus to infect its primary target cells, B lymphocytes and epithelial cells (NIH, 2024). This machinery includes the major attachment protein gp350/220, which binds to the complement receptor CD21 on B cells, and the core fusion machinery consisting of glycoproteins gH, gL, and gB (MDPI, 2024). For B cell infection, an additional glycoprotein, gp42, acts as a tropism switch by binding to HLA class II molecules to trigger fusion, whereas epithelial cell entry involves interactions between gH/gL and host integrins or ephrin receptor A2 (NIH, 2025; ResearchGate, 2023). These glycoproteins are critical therapeutic targets for the development of prophylactic and therapeutic vaccines, as well as monoclonal antibodies, aimed at preventing EBV-associated diseases (Frontiers, 2021). Current clinical candidates, such as Moderna's mRNA-1189 and NIAID's gp350-Ferritin nanoparticle vaccine, target multiple glycoproteins to block both B cell and epithelial cell entry pathways (Moderna, 2026; NIH, 2022). EBV is linked to a wide range of conditions, including infectious mononucleosis, various lymphomas, nasopharyngeal and gastric carcinomas, and autoimmune diseases like multiple sclerosis (Medium, 2026; NIH, 2023).

Other names

EBV envelope glycoproteinsEBV entry machineryEBV fusion machinerygp350/220 (BLLF1)gH/gL complex (BXLF2/BKRF2)gB (BALF4/gp110)gp42 (BZLF2)BMRF2

Neutralization of viral entry by blocking attachment to host receptors such as CD21, HLA class II, and integrins, or by inhibiting the core fusion machinery composed of gH, gL, and gB (NIH, 2024; MDPI, 2024).