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The Epstein-Barr virus (EBV) antigen–Human leukocyte antigen (HLA) class I peptide complex is a molecular assembly found on the surface of EBV-infected cells, including various types of EBV-associated lymphomas (Taylor et al., 2015). This complex consists of a viral peptide, typically derived from EBV latency proteins such as LMP1, LMP2, or EBNA1, nestled within the binding groove of an HLA class I molecule (Bollard & Heslop, 2016). Its primary biological role is to serve as a signal for the immune system, specifically allowing CD8+ cytotoxic T cells to identify and eliminate infected or malignant cells through T-cell receptor (TCR) recognition (Heslop et al., 2010). In the context of EBV-associated malignancies, these complexes are exploited as highly specific therapeutic targets for immunotherapy (Smith et al., 2015). Current clinical approaches include the use of EBV-specific T-cell therapies, such as Tabelecleucel, and TCR-engineered cells designed to bind these complexes and trigger a potent anti-tumor immune response (Atara Biotherapeutics, 2022). The specificity of this target minimizes damage to healthy non-infected cells, although therapeutic success depends on the presence of both the viral antigen and the appropriate HLA restriction element (Taylor et al., 2015).
Recognition by T-cell receptors (TCRs) on cytotoxic T lymphocytes (CTLs) leading to targeted cell lysis and cytokine release (Bollard & Heslop, 2016).
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