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Epstein-Barr virus glycoprotein 350 (gp350), also known as gp350/220, is the primary envelope glycoprotein of the Epstein-Barr virus (EBV) and is encoded by the BLLF1 gene [1, 8]. It plays a fundamental role in the viral life cycle by mediating the attachment of EBV to host B cells through its interaction with the complement receptor 2 (CR2/CD21) [1, 3, 9]. Although gp350 is primarily expressed during the lytic phase of infection, it is also found on the surface of certain EBV-positive tumor cells and can be released in extracellular vesicles, making it a specific target for immunotherapy [3, 6, 7]. Current therapeutic strategies targeting gp350 include prophylactic vaccines like mRNA-1189, which aim to prevent infection, and therapeutic approaches such as gp350-targeted CAR-T cells designed to eliminate malignant cells in EBV-associated lymphomas [3, 4, 7]. The high specificity of gp350 to EBV-infected cells provides a unique opportunity to target oncovirus-driven cancers while minimizing damage to uninfected tissues [3, 7]. Additionally, anti-gp350 antibody titers are utilized as biomarkers for monitoring infection status and assessing the risk of EBV-associated diseases like nasopharyngeal carcinoma [11, 12].
Neutralization of viral entry by blocking the interaction with CD21 (CR2) on B cells; direct cytotoxic killing of EBV-positive cells via CAR-T or antibody-dependent cellular cytotoxicity (ADCC).
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