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The LMP2 peptide–MHC-I complex refers to antigenic peptides derived from the *Epstein–Barr Virus* (EBV) **latent membrane protein 2 (LMP2)** that are processed by the immunoproteasome, loaded onto **major histocompatibility complex class I (MHC-I)** molecules, and displayed on the surface of infected cells for recognition by **CD8+ cytotoxic T lymphocytes**[3][4][5][6]. This interaction is central to immune surveillance against EBV and forms the basis for immunotherapeutic strategies targeting EBV-associated malignancies. The complex is a key element in the adaptive immune response, with documented structural insights into how TCRs recognize these peptide–MHC complexes, including unique aspects of dual peptide occupancy and novel neo-epitope generation[4]. Aberrant presentation or immune escape from this complex is linked to viral persistence and tumor immune evasion[6]. **Note:** "LMP2" is also used to refer to the β1i subunit (PSMB9) of the immunoproteasome. In the given context ("LMP2 peptide presented by MHC-I"), it specifically refers to the viral antigenic peptide from EBV (not the proteasome subunit)[3].
Recognition by cytotoxic T lymphocytes (CTLs): CD8+ T cells recognize and bind to the LMP2 peptide–MHC-I complex via their T cell receptor (TCR), leading to targeted cell killing. Immunotherapy: Engineered TCRs or T cells (e.g., TCR or CAR-T technology) can be designed to seek out cells displaying this complex for elimination in viral infection or cancer contexts.
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