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

Sebastian Joyce; 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; Onisha Patel; Lars Kjer-Nielsen; James McCluskey; Dale I. Godfrey; Jamie Rossjohn; Stewart K. Richardson; Steven A. Porcelli; Amy R. Howell; Kyoko Hayakawa; Laurent Gapin; Dirk M. Zajonc; Peng George Wang

doi:10.1038/emboj.2009.286

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

Sebastian Joyce, 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, Onisha Patel, Lars Kjer-Nielsen, James McCluskey, Dale I. Godfrey, Jamie Rossjohn, Stewart K. Richardson, Steven A. Porcelli, Amy R. Howell, Kyoko HayakawaLaurent Gapin, Dirk M. Zajonc, Peng George Wang

Microbiology & Immunology

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

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, including α-galactosylceramide, the structurally similar α-galactosyldiacylglycerol and the very distinct isoglobotriaosylceramide. We also show that the relative roles of the CDR loops within the NKTcr Β-chain varied as a function of the antigen. Thus, while NKTcrs characteristically use a conserved docking mode, the NKTcr Β-chain allows these cells to recognise unique aspects of structurally diverse CD1d-restricted ligands.

Original language	English (US)
Pages (from-to)	3579-3590
Number of pages	12
Journal	EMBO Journal
Volume	28
Issue number	22
DOIs	https://doi.org/10.1038/emboj.2009.286
State	Published - Nov 2009

Keywords

Antigen recognition
Glycolipid antigens
NKT cells
Recognition logic
Semi-invariant T-cell receptor

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
General Biochemistry, Genetics and Molecular Biology
General Immunology and Microbiology

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10.1038/emboj.2009.286

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Joyce, S., Florence, W. C., Xia, C., Gordy, L. E., Chen, W., Zhang, Y., Scott-Browne, J., Kinjo, Y., Yu, K. O. A., Keshipeddy, S., Pellicci, D. G., Patel, O., Kjer-Nielsen, L., McCluskey, J., Godfrey, D. I., Rossjohn, J., Richardson, S. K., Porcelli, S. A., Howell, A. R., ... Wang, P. G. (2009). Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands. EMBO Journal, 28(22), 3579-3590. https://doi.org/10.1038/emboj.2009.286

Joyce, S, Florence, WC, Xia, C, Gordy, LE, Chen, W, Zhang, Y, Scott-Browne, J, Kinjo, Y, Yu, KOA, Keshipeddy, S, Pellicci, DG, Patel, O, Kjer-Nielsen, L, McCluskey, J, Godfrey, DI, Rossjohn, J, Richardson, SK, Porcelli, SA, Howell, AR, Hayakawa, K, Gapin, L, Zajonc, DM & Wang, PG 2009, 'Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands', EMBO Journal, vol. 28, no. 22, pp. 3579-3590. https://doi.org/10.1038/emboj.2009.286

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

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, including α-galactosylceramide, the structurally similar α-galactosyldiacylglycerol and the very distinct isoglobotriaosylceramide. We also show that the relative roles of the CDR loops within the NKTcr Β-chain varied as a function of the antigen. Thus, while NKTcrs characteristically use a conserved docking mode, the NKTcr Β-chain allows these cells to recognise unique aspects of structurally diverse CD1d-restricted ligands.",

keywords = "Antigen recognition, Glycolipid antigens, NKT cells, Recognition logic, Semi-invariant T-cell receptor",

author = "Sebastian Joyce and Florence, {William C.} and Chengfeng Xia and Gordy, {Laura E.} and Wenlan Chen and Yalong Zhang and James Scott-Browne and Yuki Kinjo and Yu, {Karl O.A.} and Santosh Keshipeddy and Pellicci, {Daniel G.} and Onisha Patel and Lars Kjer-Nielsen and James McCluskey and Godfrey, {Dale I.} and Jamie Rossjohn and Richardson, {Stewart K.} and Porcelli, {Steven A.} and Howell, {Amy R.} and Kyoko Hayakawa and Laurent Gapin and Zajonc, {Dirk M.} and Wang, {Peng George}",

year = "2009",

month = nov,

doi = "10.1038/emboj.2009.286",

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AU - Joyce, Sebastian

AU - Florence, William C.

AU - Xia, Chengfeng

AU - Gordy, Laura E.

AU - Chen, Wenlan

AU - Zhang, Yalong

AU - Scott-Browne, James

AU - Kinjo, Yuki

AU - Yu, Karl O.A.

AU - Keshipeddy, Santosh

AU - Pellicci, Daniel G.

AU - Patel, Onisha

AU - Kjer-Nielsen, Lars

AU - McCluskey, James

AU - Godfrey, Dale I.

AU - Rossjohn, Jamie

AU - Richardson, Stewart K.

AU - Porcelli, Steven A.

AU - Howell, Amy R.

AU - Hayakawa, Kyoko

AU - Gapin, Laurent

AU - Zajonc, Dirk M.

AU - Wang, Peng George

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N2 - 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, including α-galactosylceramide, the structurally similar α-galactosyldiacylglycerol and the very distinct isoglobotriaosylceramide. We also show that the relative roles of the CDR loops within the NKTcr Β-chain varied as a function of the antigen. Thus, while NKTcrs characteristically use a conserved docking mode, the NKTcr Β-chain allows these cells to recognise unique aspects of structurally diverse CD1d-restricted ligands.

AB - 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, including α-galactosylceramide, the structurally similar α-galactosyldiacylglycerol and the very distinct isoglobotriaosylceramide. We also show that the relative roles of the CDR loops within the NKTcr Β-chain varied as a function of the antigen. Thus, while NKTcrs characteristically use a conserved docking mode, the NKTcr Β-chain allows these cells to recognise unique aspects of structurally diverse CD1d-restricted ligands.

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

Abstract

Keywords

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