T cell receptor reversed polarity recognition of a self-antigen major histocompatibility complex View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-11

AUTHORS

Dennis X Beringer, Fleur S Kleijwegt, Florian Wiede, Arno R van der Slik, Khai Lee Loh, Jan Petersen, Nadine L Dudek, Gaby Duinkerken, Sandra Laban, Antoinette Joosten, Julian P Vivian, Zhenjun Chen, Adam P Uldrich, Dale I Godfrey, James McCluskey, David A Price, Kristen J Radford, Anthony W Purcell, Tatjana Nikolic, Hugh H Reid, Tony Tiganis, Bart O Roep, Jamie Rossjohn

ABSTRACT

Central to adaptive immunity is the interaction between the αβ T cell receptor (TCR) and peptide presented by the major histocompatibility complex (MHC) molecule. Presumably reflecting TCR-MHC bias and T cell signaling constraints, the TCR universally adopts a canonical polarity atop the MHC. We report the structures of two TCRs, derived from human induced T regulatory (iT(reg)) cells, complexed to an MHC class II molecule presenting a proinsulin-derived peptide. The ternary complexes revealed a 180° polarity reversal compared to all other TCR-peptide-MHC complex structures. Namely, the iT(reg) TCR α-chain and β-chain are overlaid with the α-chain and β-chain of MHC class II, respectively. Nevertheless, this TCR interaction elicited a peptide-reactive, MHC-restricted T cell signal. Thus TCRs are not 'hardwired' to interact with MHC molecules in a stereotypic manner to elicit a T cell signal, a finding that fundamentally challenges our understanding of TCR recognition. More... »

PAGES

1153-1161

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ni.3271

    DOI

    http://dx.doi.org/10.1038/ni.3271

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1040464787

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26437244


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