Epstein-Barr virus glycoproteins gp350, gH, gL, and gp42 (EBV gp350/gH/gL/gp42)

The Epstein-Barr virus (EBV) glycoproteins gp350, gH, gL, and gp42 constitute the essential machinery for viral attachment and entry into host cells [2, 3]. Gp350 is the most abundant envelope protein and mediates initial attachment to B cells by binding to the complement receptor CD21 [2, 14]. The gH/gL heterodimer forms the core fusion apparatus, which is conserved across herpesviruses, while gp42 acts as a molecular switch that facilitates B-cell infection by binding to HLA class II molecules [5, 16]. Interestingly, gp42 inhibits infection of epithelial cells, where entry is instead mediated by the gH/gL complex interacting with cellular integrins [4, 16]. These glycoproteins are the primary targets for prophylactic vaccines and therapeutic monoclonal antibodies aimed at preventing infectious mononucleosis and EBV-associated malignancies such as Burkitt lymphoma and nasopharyngeal carcinoma [9, 12]. Current drug development efforts focus on neutralizing these proteins to block viral entry and reduce the global burden of EBV-related diseases, including its recently confirmed role in multiple sclerosis [10, 17].

Other names

BLLF1 (gp350)BKRF2 (gH)BLLF2 (gL)BZLF2 (gp42)gp350/220gp85 (gH)gp25 (gL)EBV entry complexEBV fusion machinery

Neutralization of viral entry by blocking attachment to host receptors (CD21, HLA class II) and inhibiting membrane fusion mediated by the gH/gL/gp42 complex.