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• W2024294539 startingPage "370" @default.
• W2024294539 abstract "T-cell receptors (TCR) recognize peptides complexed to self-major histocompatibility complex (MHC) molecules. Recognition of peptide/MHC ligands by the TCR is highly peptide specific. However, certain TCRs can also recognize sequence-related and -unrelated ('mimicry') epitopes presented by homologous MHC molecules. Using two human, human leucocyte antigen-DR1 (HLA-DR1)-restricted T-cell clones specific for HA p307-319, we identified several diverse combinations of peptide-MHC complexes that are functionally equivalent in their ability to trigger T-cell stimulation. These findings demonstrate that a single TCR can productively interact with different peptides complexed to self- as well as non-self-MHC molecules. This extended reactivity is human leucocyte antigen (HLA) allele and TCR clonotype dependent, as the peptide repertoire recognized depends on the presenting HLA-DR molecule and varies among different TCRs that both recognize the HA p307-319/DR1 complex. Importantly, certain peptide analogues can completely change the HLA-restriction pattern of the TCR: T-cell recognition of the wild-type peptide that was absent in the context of a non-self HLA-DR molecule, was restored by complementing substitutions in altered peptide ligands, that could not be presented by the original restriction element. This mechanism may play an important role in allorecognition." @default.
• W2024294539 created "2016-06-24" @default.
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• W2024294539 date "1997-03-01" @default.
• W2024294539 modified "2023-10-13" @default.
• W2024294539 title "Flexibility in T-cell receptor ligand repertoires depends on MHC and T-cell receptor clonotype" @default.
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• W2024294539 doi "https://doi.org/10.1111/j.1365-2567.1997.00370.x" @default.
• W2024294539 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1456601" @default.
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