Epstein-Barr virus surface glycoproteins (EBV glycoproteins)

Epstein-Barr virus (EBV) surface glycoproteins are a complex of envelope proteins that mediate the virus's attachment and entry into host cells, specifically B lymphocytes and epithelial cells (Sathiyamoorthy et al., 2017, Current Opinion in Virology). The primary attachment protein, gp350 (encoded by BLLF1), binds to the CD21 receptor on B cells, while the gH/gL complex and gB (BALF4) are essential for the subsequent fusion of the viral envelope with the host cell membrane (Young et al., 2007, Nature Reviews Cancer). These glycoproteins are critical therapeutic targets because they are the primary antigens for neutralizing antibodies that can prevent infection. EBV is a ubiquitous human herpesvirus associated with infectious mononucleosis and several cancers, including Burkitt lymphoma, Hodgkin lymphoma, and nasopharyngeal carcinoma, as well as a significantly increased risk of developing multiple sclerosis (Bjornevik et al., 2022, Science). Current drug development focuses on prophylactic vaccines, such as mRNA-1189, which targets multiple glycoproteins to elicit a broad immune response, and monoclonal antibodies designed to block viral entry (Moderna, 2024; NIH, 2023). Targeting these proteins aims to reduce the viral load and prevent the establishment of latent infection, which is the precursor to EBV-associated malignancies and autoimmune complications (Cohen, 2015, Journal of Clinical Investigation).

Other names

EBV envelope glycoproteinsgp350/220gH/gL complexgB (BALF4)gp42 (BZLF2)BLLF1BKRF1BLLF2

Neutralization of viral entry and inhibition of viral attachment to host cells