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The **tumor cell neoantigen peptide–HLA complex** is composed of a peptide derived from tumor-specific mutations (neoantigen) bound within the peptide-binding groove of a human leukocyte antigen (HLA) molecule on the cell surface. Recognition of these complexes by T cell receptors is central to immune-mediated elimination of cancer cells and underlies multiple therapeutic strategies, including adoptive T cell transfer, personalized cancer vaccines, and TCR-mimic antibodies. Immunogenicity depends on the unique structure of the presented peptide, the patient’s HLA genotype, and the affinity and specificity of the TCR. Therapeutic exploitation of these complexes enables patient- and tumor-specific precision immunotherapy, but challenges remain due to tumor heterogeneity, immune editing, and the risk of unintended cross-reactivity or immune escape[2][3][5][1][7].
Direct targeting of tumor cells by TCRs recognizing neoantigen peptide–HLA complexes, leading to T-cell-mediated cytotoxicity\nInduction of tumor-specific immune responses (vaccines present neoantigen peptides to HLA for immune priming[5][6][7])\nAntibody-based therapies mimicking TCR recognition of these complexes
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