Journal article
Vβ2 natural killer T cell antigen receptor-mediated recognition of CD1d-glycolipid antigen
O Patel, DG Pellicci, AP Uldrich, LC Sullivan, M Bhati, M McKnight, SK Richardson, AR Howell, T Mallevaey, J Zhang, R Bedel, GS Besra, AG Brooks, L Kjer-Nielsen, J McCluskey, SA Porcelli, L Gapin, J Rossjohn, DI Godfrey
Proceedings of the National Academy of Sciences of the United States of America | Published : 2011
Abstract
Natural killer T cell antigen receptors (NKT TCRs) recognize lipidbased antigens (Ags) presented by CD1d. Although the TCR α-chain is invariant, NKT TCR Vβ exhibits greater diversity, with one (Vβ11) and three (Vβ8, Vβ7, and Vβ2) Vβ chains in humans and mice, respectively. With the exception of the Vβ2 NKT TCR, NKT TCRs possess canonical tyrosine residues within complementarity determining region (CDR) 2β that are critical for CD1d binding. Thus, how Vβ2 NKT TCR docks with CD1d-Ag was unclear. Despite the absence of the CDR2β-encoded tyrosine residues, we show that the Vβ2 NKT TCR engaged CD1d-Ag in a similar manner and with a comparable affinity and energetic footprint to the manner observe..
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Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
We thank the staff at the MX2 beamline of the Australian synchrotron for assistance with data collection; Meena Thakur for the gift of the 4',4 ''-deoxy alpha-GalCer analogue; and Christina Wang and Maria Sandoval for technical assistance. This work was supported in part by the Australian Research Council (ARC), the National Health and Medical Research Council of Australia (NHMRC), and the Cancer Council of Victoria; National Institutes of Health (NIH)/National Institute of General Medical Sciences Grant GM087136 (to A. R. H.); NIH Grant AI45889 (to S. A. P.); NIH Grant AI057485 (to L. G.); an ARC Federation Fellowship (to J.R.); and an NHMRC Principal Research Fellowship (to D.I.G.).