Epstein-Barr virus envelope proteins (EBV envelope proteins)

Epstein-Barr virus (EBV) envelope proteins are a complex group of surface glycoproteins critical for the virus's ability to attach to, fuse with, and enter human host cells [3, 8, 16]. The primary proteins involved include gp350/220, which facilitates initial attachment to B cells via the CD21 (CR2) receptor, and the core fusion machinery consisting of glycoprotein B (gB) and the glycoprotein H/L (gH/gL) complex [4, 10, 26]. B-cell entry requires an additional cofactor, gp42, which interacts with MHC class II molecules, while epithelial cell infection is mediated by gH/gL binding to integrins and EphA2 [9, 14, 23]. These proteins are major therapeutic targets for vaccines and monoclonal antibodies aimed at preventing primary EBV infection and its associated pathologies, including infectious mononucleosis, several lymphoid and epithelial malignancies, and autoimmune diseases such as multiple sclerosis [13, 17, 18, 20]. Current pharmacological strategies involve neutralizing these proteins to block the viral entry cycle, with several mRNA-based vaccines and neutralizing monoclonal antibodies currently in clinical and preclinical development [6, 13, 16, 23].

Other names

Epstein-Barr virus glycoproteinsEBV surface proteinsgp350/220 (BLLF1)Glycoprotein B (gB, BALF4)Glycoprotein H (gH, BXLF2)Glycoprotein L (gL, BKRF2)Glycoprotein gp42 (BZLF2)

Virus neutralization, inhibition of viral entry into host cells, and blocking of membrane fusion machinery