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EMBO Press, The EMBO Journal, 22(28), p. 3579-3590

DOI: 10.1038/emboj.2009.286

EMBO Press, The EMBO Journal, 23(28), p. 3781-3781

DOI: 10.1038/emboj.2009.348

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Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands

Journal article published in 2009 by William C. Florence, Chengfeng Xia, Laura E. Gordy, Wenlan Chen, Yalong Zhang, James Scott-Browne, Yuki Kinjo, Karl O. A. Yu, Santosh Keshipeddy, Daniel G. Pellicci ORCID, Onisha Patel, Lars Kjer-Nielsen, James McCluskey, Dale I. Godfrey, Jamie Rossjohn and other authors.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The semi-invariant natural killer (NK) T-cell receptor (NKTcr) recognises structurally diverse glycolipid antigens presented by the monomorphic CD1d molecule. While the alpha-chain of the NKTcr is invariant, the beta-chain is more diverse, but how this diversity enables the NKTcr to recognise diverse antigens, such as an alpha-linked monosaccharide (alpha-galactosylceramide and alpha-galactosyldiacylglycerol) and the beta-linked trisaccharide (isoglobotriaosylceramide), is unclear. We demonstrate here that NKTcrs, which varied in their beta-chain usage, recognised diverse glycolipid antigens with a similar binding mode on CD1d. Nevertheless, the NKTcrs recognised distinct epitopic sites within these antigens, including alpha-galactosylceramide, the structurally similar alpha-galactosyldiacylglycerol and the very distinct isoglobotriaosylceramide. We also show that the relative roles of the CDR loops within the NKTcr beta-chain varied as a function of the antigen. Thus, while NKTcrs characteristically use a conserved docking mode, the NKTcr beta-chain allows these cells to recognise unique aspects of structurally diverse CD1d-restricted ligands.