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Epstein-Barr virus envelope glycoprotein gp350 is the major envelope protein encoded by the BLLF1 gene of Epstein-Barr virus (EBV) and is the most abundant glycoprotein on the virus surface[2][5]. gp350 mediates the initial attachment of EBV to host B lymphocytes by binding the complement receptor 2 (CR2, also known as CD21) on the B cell surface, a critical step for infection initiation[1][3][5]. Structural studies demonstrate a specific electrostatically driven interaction, with implications for host selectivity and tropism. gp350 is also a primary target of neutralizing antibodies and is being explored as an antigen for vaccines and antibody therapies designed to prevent EBV infection and its associated malignancies (such as B cell lymphomas)[1][2]. While not a host receptor, gp350 is a validated viral target due to its essential role in infection of B cells[1][2][5].
Antibodies block gp350 binding to CR2, neutralizing EBV infection of B cells
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