Epstein-Barr virus envelope glycoprotein complex (EBV glycoproteins) (EBV glycoproteins)

The Epstein-Barr virus (EBV) envelope glycoprotein complex consists of several key proteins, including gp350, gB, gH, gL, and gp42, which collectively mediate viral attachment and membrane fusion into host cells (Sathiyamoorthy et al., 2017, Nature Communications). gp350 is the most abundant surface protein and facilitates initial tethering to B cells via the CD21 receptor (Young et al., 2007, Nature Reviews Cancer). The core fusion machinery, composed of gH/gL and gB, is triggered by specific interactions: gp42 binds to MHC class II for B cell entry, while gH/gL interacts directly with integrins for epithelial cell entry (Chesnokova et al., 2013, Journal of Virology). These proteins are critical therapeutic targets because neutralizing antibodies against them can prevent primary infection and subsequent EBV-associated malignancies such as Burkitt lymphoma and nasopharyngeal carcinoma (Cohen, 2015, Current Opinion in Virology). Current drug development focuses on multi-component vaccines, such as mRNA-1189, and monoclonal antibodies like AMMO1 that target the gH/gL complex to block entry into both B cells and epithelial cells (Snijder et al., 2018, Immunity).

Other names

gp350 (BLLF1)gp220gH/gL complex (BKRF2/BLLF2)Glycoprotein B (gB, BALF4)gp42 (BZLF2)EBV entry machinery

Neutralization of viral entry by blocking attachment to host receptors or inhibiting the conformational changes required for membrane fusion (Sathiyamoorthy et al., 2017).