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- W4385686083 abstract "Abstract Noncovalent bonds typically mediate interactions between a T cell receptor (TCR) and a peptide-major histocompatibility complex (pMHC) ligand. In this study, we describe a novel mechanism involving a covalent TCR-pMHC interaction through a cysteine-cysteine disulfide bond. By introducing cysteine resodues into the TCR CDR3 and into the peptide of a known TCR-pMHC combination, we show that this disulfide bond formation does not require structural rearrangement and can still occur even when the initial affinity of the TCR-pMHC interaction is low. This mechanism strongly activates TCR signaling and has potential applications in basic immunology to further our fundamental understanding of T cell activation/differentiation as well as applied clinically for improving the efficacy and sensitivity of adoptive T cell therapies. Our findings shed new light on T cell activation and provide additional avenues for the development of modern immunotherapy." @default.
- W4385686083 created "2023-08-10" @default.
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- W4385686083 date "2023-05-01" @default.
- W4385686083 modified "2023-09-27" @default.
- W4385686083 title "Covalent TCR-pMHC Interactions: A New Mechanism for T Cell Antigen Recognition and T cell Activation" @default.
- W4385686083 doi "https://doi.org/10.4049/jimmunol.210.supp.76.18" @default.
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