Envelope glycoprotein GP350 (gp350) (gp350/220)

The Epstein-Barr virus (EBV) envelope glycoprotein GP350/220, encoded by the BLLF1 gene, is the most abundant protein on the viral surface and serves as the primary mediator for infection of B-lymphocytes (UniProt P03200). It functions by binding to the complement receptor type 2 (CD21/CR2) or CD35 (CR1) on the surface of B cells, an interaction that initiates viral attachment and subsequent entry (PubMed 2987520). While GP350 is the full-length form, GP220 is a shorter splice variant that retains the receptor-binding domain (PubMed 6087149). This glycoprotein is a major target for the host's neutralizing antibody response and has been the central focus of EBV vaccine development for decades (PubMed 12771413). Clinically, GP350/220 is associated with the pathogenesis of infectious mononucleosis and various EBV-linked malignancies, including Burkitt lymphoma, Hodgkin lymphoma, and nasopharyngeal carcinoma, as well as autoimmune conditions like multiple sclerosis (PubMed 1.1.4, 1.5.3). Therapeutic strategies targeting this protein include recombinant subunit vaccines, nanoparticle-based vaccines, and monoclonal antibodies designed to block viral entry (NCT05164094, NCT04645147). Although GP350-based vaccines have shown success in reducing the incidence of symptomatic infectious mononucleosis in clinical trials, they often fail to provide sterilizing immunity against the virus itself (PubMed 1.5.3, 1.5.5). Furthermore, some research suggests that anti-GP350 antibodies might paradoxically enhance the infection of epithelial cells, presenting a challenge for comprehensive EBV prophylaxis (PubMed 1.4.1).

Other names

gp350gp220BLLF1Membrane antigenMAgp340

Neutralization of viral attachment to B-lymphocytes by blocking the interaction between gp350 and the host receptor CD21 (CR2).