| Literature DB >> 31857486 |
Jérôme Le Nours1,2, Nicholas A Gherardin3,4, Sri H Ramarathinam1, Wael Awad1, Florian Wiede1,5, Benjamin S Gully1,2, Yogesh Khandokar1, T Praveena1, Jacinta M Wubben1, Jarrod J Sandow6,7, Andrew I Webb6,7, Anouk von Borstel1,2, Michael T Rice1,2, Samuel J Redmond3, Rebecca Seneviratna3, Maria L Sandoval-Romero1, Shihan Li3,4, Michael N T Souter3, Sidonia B G Eckle3, Alexandra J Corbett3, Hugh H Reid1,2, Ligong Liu8,9, David P Fairlie8,9, Edward M Giles10, Glen P Westall11,12, Richard W Tothill13,14, Martin S Davey1,2, Richard Berry1,2, Tony Tiganis1,5, James McCluskey3, Daniel G Pellicci3,4, Anthony W Purcell1, Adam P Uldrich3,4, Dale I Godfrey15,4, Jamie Rossjohn16,2,17.
Abstract
T cell receptors (TCRs) recognize antigens presented by major histocompatibility complex (MHC) and MHC class I-like molecules. We describe a diverse population of human γδ T cells isolated from peripheral blood and tissues that exhibit autoreactivity to the monomorphic MHC-related protein 1 (MR1). The crystal structure of a γδTCR-MR1-antigen complex starkly contrasts with all other TCR-MHC and TCR-MHC-I-like complex structures. Namely, the γδTCR binds underneath the MR1 antigen-binding cleft, where contacts are dominated by the MR1 α3 domain. A similar pattern of reactivity was observed for diverse MR1-restricted γδTCRs from multiple individuals. Accordingly, we simultaneously report MR1 as a ligand for human γδ T cells and redefine the parameters for TCR recognition.Entities:
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Year: 2019 PMID： 31857486 DOI： 10.1126/science.aav3900
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728