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The neoantigen–major histocompatibility complex class I complex (neoantigen–MHC-I) refers to the structure formed when a novel, tumor-specific peptide ("neoantigen") is processed inside a cell and presented at the cell surface bound to an MHC class I molecule. This complex is recognized specifically by cytotoxic CD8+ T cells, which can then eliminate abnormal or cancerous cells expressing these neoantigens. The formation and surface display of pMHC-I complexes are central to anti-tumor immune surveillance and the efficacy of cancer immunotherapies. Cancers and viruses can evade immune detection by loss or alteration of this pathway, making restoration or targeting of neoantigen–MHC-I complexes a major therapeutic goal[1][2][3][4][5][7][8]. Note: There is no single "canonical" gene or protein for the "neoantigen–MHC class I complex": - MHC class I molecules: encoded by HLA-A, HLA-B, and HLA-C in humans - Neoantigens: derived from mutated or abnormal proteins, and thus are not encoded by a single sequence - The "target" is the specific peptide–MHC-I complex, which means it is a context-dependent, highly variable molecular structure[4][5][7]. If you need information on a specific HLA molecule or a specified neoantigen, a more precise target identifier is required.
T-cell recognition and killing (drugs and therapies that enhance CD8+ T cell activity depend on pMHC-I presentation of neoantigens) Immune checkpoint blockade (enables T cells to respond to pMHC-I–bearing cells by inhibiting negative regulatory signals)
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