Epstein-Barr virus glycoprotein 350–Complement receptor type 2 interface (EBV gp350–CR2 interface)

The Epstein-Barr virus (EBV) gp350–CR2/CD21 interface is a critical protein-protein interaction site that mediates the primary attachment of EBV to host B lymphocytes. The viral envelope glycoprotein gp350 (encoded by the BLLF1 gene) binds with high affinity to the complement receptor type 2 (CR2/CD21) on the surface of B cells, initiating the process of viral tethering and subsequent membrane fusion. This interaction is the most abundant and immunodominant target on the EBV virion, making it a focal point for the development of neutralizing antibodies and prophylactic vaccines. Disrupting this interface prevents the virus from infecting B cells, which is essential for controlling both primary infection (infectious mononucleosis) and EBV-associated malignancies such as Burkitt lymphoma and nasopharyngeal carcinoma. Research into this target involves structural biology to map the precise binding residues and the development of biologics that can mimic or block the CR2-binding domain of gp350.

Other names

gp350-CD21 interfaceEBV gp350-CR2 binding siteBLLF1-CR2 interaction siteEpstein-Barr virus attachment interface

Inhibition of viral attachment to host B cells by blocking the interaction between the viral gp350 protein and the host CR2/CD21 receptor, thereby preventing viral entry and subsequent infection.