Journal article
Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands
S Joyce, WC Florence, C Xia, LE Gordy, W Chen, Y Zhang, J Scott-Browne, Y Kinjo, KOA Yu, S Keshipeddy, DG Pellicci, O Patel, L Kjer-Nielsen, J McCluskey, DI Godfrey, J Rossjohn, SK Richardson, SA Porcelli, AR Howell, K Hayakawa Show all
EMBO Journal | WILEY | Published : 2009
Abstract
The semi-invariant natural killer (NK) T-cell receptor (NKTcr) recognises structurally diverse glycolipid antigens presented by the monomorphic CD1d molecule. While the α-chain of the NKTcr is invariant, the Β-chain is more diverse, but how this diversity enables the NKTcr to recognise diverse antigens, such as an α-linked monosaccharide (α-galactosylceramide and α-galactosyldiacylglycerol) and the Β-linked trisaccharide (isoglobotriaosylceramide), is unclear. We demonstrate here that NKTcrs, which varied in their Β-chain usage, recognised diverse glycolipid antigens with a similar binding mode on CD1d. Nevertheless, the NKTcrs recognised distinct epitopic sites within these antigens, includ..
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Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
We thank L Van Kaer for critical evaluation of the data and helpful suggestions on the writing of this paper. This work was supported by grants from the NIH HL069765 (WCF, LEG) AI007611 (LEG), AI45889 (SAP), AI057519 (ARH), AI074952 (DMZ), AI048224 and AI061721 (SJ), as well as by the Medical Scientist Training Program of the Albert Einstein College of Medicine (KAOY), the Cancer Research Institute's Investigator Award (DMZ) and an endowment from the Ohio State University (PGW).