Epstein-Barr virus glycoprotein gp350 (gp350) (gp350)

Epstein-Barr virus (EBV) glycoprotein gp350, encoded by the BLLF1 gene, is the most abundant protein on the viral envelope and serves as the primary mediator for viral attachment to host B lymphocytes (UniProt P03200). It specifically binds to the Complement Receptor 2 (CR2/CD21) on the surface of B cells, initiating the process of viral entry and infection (PMID: 17227428). Because of its critical role in the EBV life cycle and its high expression levels, gp350 is a major target for the development of prophylactic vaccines and therapeutic monoclonal antibodies (PMID: 27121251). Neutralizing antibodies directed against the CR2-binding site of gp350 can prevent the virus from infecting B cells, thereby potentially reducing the incidence of infectious mononucleosis and EBV-associated malignancies such as Burkitt lymphoma and post-transplant lymphoproliferative disorder (NIH, 2022). Current research also explores the link between EBV infection and autoimmune conditions like multiple sclerosis, further highlighting gp350 as a significant therapeutic target (Moderna, 2023). While gp350 is highly immunogenic, its extensive O-linked glycosylation can act as a glycan shield, which may complicate the development of broadly effective vaccines by masking key epitopes.

Other names

gp340BLLF1Major envelope glycoprotein gp350/220EBV gp350Epstein-Barr virus membrane antigen

Drugs targeting this site function primarily by blocking the physical interaction between the viral gp350 protein and the host CD21 receptor, thereby neutralizing the virus's ability to attach to and infect B lymphocytes.