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• W2889980427 abstract "T cell receptor cross-reactivity allows a fixed T cell repertoire to respond to a much larger universe of potential antigens. Recent work has emphasized the importance of peptide structural and chemical homology, as opposed to sequence similarity, in T cell receptor cross-reactivity. Surprisingly, though, T cell receptors can also cross-react between ligands with little physiochemical commonalities. Studying the clinically relevant receptor DMF5, we demonstrate that cross-recognition of such divergent antigens can occur through mechanisms that involve heretofore unanticipated rearrangements in the peptide and presenting MHC protein, including binding-induced peptide register shifts and extensions from MHC peptide binding grooves. Moreover, cross-reactivity can proceed even when such dramatic rearrangements do not translate into structural or chemical molecular mimicry. Beyond demonstrating new principles of T cell receptor cross-reactivity, our results have implications for efforts to predict and control T cell specificity and cross-reactivity and highlight challenges associated with predicting T cell reactivities. Structural analysis shows that cross-reactivity of the T cell receptor DMF5 is governed by adaptability of the peptide antigen, which can undergo TCR-binding-induced frameshifting forcing the peptide C terminus to extend from the MHC-binding groove." @default.
• W2889980427 created "2018-09-27" @default.
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• W2889980427 date "2018-09-17" @default.
• W2889980427 modified "2023-10-17" @default.
• W2889980427 title "T cell receptor cross-reactivity expanded by dramatic peptide–MHC adaptability" @default.
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• W2889980427 doi "https://doi.org/10.1038/s41589-018-0130-4" @default.
• W2889980427 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6371774" @default.
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