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Epstein-Barr virus (EBV) glycoprotein 220 (gp220) is a major envelope protein and a splice variant of the larger gp350 protein, both encoded by the BLLF1 gene (UniProt E2GKT8). It plays a critical role in the initial stages of EBV infection by mediating the attachment of the virus to B lymphocytes through its interaction with the host cell receptor CD21, also known as complement receptor 2 (NIH PMC8231001). Because of its abundance on the viral surface and its essential role in B-cell entry, gp220 is a primary target for the development of prophylactic vaccines and neutralizing antibodies (NIH PMC5441348). While targeting gp220 can effectively prevent B-cell infection and reduce the incidence of infectious mononucleosis, it may not fully prevent infection of epithelial cells, which utilize different entry mechanisms (Frontiers in Immunology, 2021). Current therapeutic strategies, such as Moderna's mRNA-1189 vaccine candidate, aim to elicit robust humoral responses against gp220 and other glycoproteins to provide protection against EBV-associated diseases, including various lymphomas and multiple sclerosis (Drug-Dev.com, 2022).
Neutralization of viral entry into B cells by blocking the interaction between viral gp220 and the host receptor CD21 (CR2).
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