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T-cell receptors that recognize MUC1 or WT1 peptide-MHC complexes are membrane-bound immune receptors on the surface of T lymphocytes. These TCRs specifically bind to peptide fragments derived from the tumor-associated antigens MUC1 or WT1 presented by major histocompatibility complex (MHC, also known as HLA in humans) molecules on antigen-presenting cells or tumor cells[1][2][3]. Recognition of these peptide-MHC complexes leads to activation of T cells, triggering cytotoxic responses against cancer cells expressing MUC1 or WT1 peptides. This process forms the basis for targeted immunotherapies, such as engineered TCR therapies and TCR-mimetic antibodies,[3][6] which aim to selectively harness immune responses against cancer cells overexpressing these antigens. MUC1 and WT1 are widely studied cancer antigens considered promising targets for immunotherapy, but safety and cross-reactivity must be carefully managed to avoid adverse effects[4].
Antigen recognition: TCR binds to MHC-loaded tumor peptide (MUC1 or WT1), leading to T-cell activation, cytokine release, and cytotoxic killing of presenting tumor cell[1][3] Immune cell recruitment and effector function activation
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