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Volumn 394, Issue 1, 2009, Pages 71-82

Structural Evaluation of Potent NKT Cell Agonists: Implications for Design of Novel Stimulatory Ligands

Author keywords

CD1; glycolipids; immune system; NKT cells; GalCer analogues

Indexed keywords

ALPHA GALACTOSYLCERAMIDE; CD1D ANTIGEN; CYTOKINE; FATTY ACID; GALACTOSE; GLYCOLIPID; LIGAND; SPHINGOSINE; T LYMPHOCYTE RECEPTOR; T LYMPHOCYTE RECEPTOR ALPHA CHAIN; T LYMPHOCYTE RECEPTOR BETA CHAIN;

EID: 70350135734     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.061     Document Type: Article
Times cited : (40)

References (36)
  • 1
    • 36448952375 scopus 로고    scopus 로고
    • CD1 antigen presentation: how it works
    • Barral D.C., and Brenner M.B. CD1 antigen presentation: how it works. Nat. Rev., Immunol. 7 (2007) 929-941
    • (2007) Nat. Rev., Immunol. , vol.7 , pp. 929-941
    • Barral, D.C.1    Brenner, M.B.2
  • 2
    • 10044286529 scopus 로고    scopus 로고
    • Going both ways: immune regulation via CD1d-dependent NKT cells
    • Godfrey D.I., and Kronenberg M. Going both ways: immune regulation via CD1d-dependent NKT cells. J. Clin. Invest. 114 (2004) 1379-1388
    • (2004) J. Clin. Invest. , vol.114 , pp. 1379-1388
    • Godfrey, D.I.1    Kronenberg, M.2
  • 4
    • 0030696696 scopus 로고    scopus 로고
    • CD1d-restricted and TCR-mediated activation of Vα14 NKT cells by glycosylceramides
    • Kawano T., Cui J., Koezuka Y., Toura I., Kaneko Y., Motoki K., et al. CD1d-restricted and TCR-mediated activation of Vα14 NKT cells by glycosylceramides. Science 278 (1997) 1626-1629
    • (1997) Science , vol.278 , pp. 1626-1629
    • Kawano, T.1    Cui, J.2    Koezuka, Y.3    Toura, I.4    Kaneko, Y.5    Motoki, K.6
  • 5
    • 18044392378 scopus 로고    scopus 로고
    • Immunotherapeutic potential for ceramide-based activators of iNKT cells
    • Berkers C.R., and Ovaa H. Immunotherapeutic potential for ceramide-based activators of iNKT cells. Trends Pharmacol. Sci. 26 (2005) 252-257
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 252-257
    • Berkers, C.R.1    Ovaa, H.2
  • 6
    • 11244304412 scopus 로고    scopus 로고
    • α-Galactosylceramide therapy for autoimmune diseases: prospects and obstacles
    • Van Kaer L. α-Galactosylceramide therapy for autoimmune diseases: prospects and obstacles. Nat. Rev., Immunol. 5 (2005) 31-42
    • (2005) Nat. Rev., Immunol. , vol.5 , pp. 31-42
    • Van Kaer, L.1
  • 7
    • 17144374753 scopus 로고    scopus 로고
    • Toward an understanding of NKT cell biology: progress and paradoxes
    • Kronenberg M. Toward an understanding of NKT cell biology: progress and paradoxes. Annu. Rev. Immunol. 23 (2005) 877-900
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 877-900
    • Kronenberg, M.1
  • 9
    • 23944448650 scopus 로고    scopus 로고
    • Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor
    • Zajonc D.M., Cantu C., Mattner J., Zhou D., Savage P.B., Bendelac A., et al. Structure and function of a potent agonist for the semi-invariant natural killer T cell receptor. Nat. Immunol. 6 (2005) 810-818
    • (2005) Nat. Immunol. , vol.6 , pp. 810-818
    • Zajonc, D.M.1    Cantu, C.2    Mattner, J.3    Zhou, D.4    Savage, P.B.5    Bendelac, A.6
  • 10
    • 0030826423 scopus 로고    scopus 로고
    • Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove
    • Zeng Z.-H., Castano A.R., Segelke B.W., Stura E.A., Peterson P.A., and Wilson I.A. Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove. Science 277 (1997) 339-345
    • (1997) Science , vol.277 , pp. 339-345
    • Zeng, Z.-H.1    Castano, A.R.2    Segelke, B.W.3    Stura, E.A.4    Peterson, P.A.5    Wilson, I.A.6
  • 11
    • 28544442722 scopus 로고    scopus 로고
    • Structural basis for CD1d presentation of sulfatide derived myelin and its implications for autoimmunity
    • Zajonc D.M., Maricic I., Wu D., Halder R., Roy K., Wong C.-H., et al. Structural basis for CD1d presentation of sulfatide derived myelin and its implications for autoimmunity. J. Exp. Med. 202 (2005) 1517-1526
    • (2005) J. Exp. Med. , vol.202 , pp. 1517-1526
    • Zajonc, D.M.1    Maricic, I.2    Wu, D.3    Halder, R.4    Roy, K.5    Wong, C.-H.6
  • 12
    • 33645235440 scopus 로고    scopus 로고
    • Design of natural killer T cell activators: structure and function of a microbial glycosphingolipid bound to mouse CD1d
    • Wu D., Zajonc D.M., Fujio M., Sullivan B.A., Kinjo Y., Kronenberg M., et al. Design of natural killer T cell activators: structure and function of a microbial glycosphingolipid bound to mouse CD1d. Proc. Natl. Acad. Sci. USA 103 (2006) 3972-3977
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3972-3977
    • Wu, D.1    Zajonc, D.M.2    Fujio, M.3    Sullivan, B.A.4    Kinjo, Y.5    Kronenberg, M.6
  • 13
    • 40449124555 scopus 로고    scopus 로고
    • Crystal structures of mouse CD1d-iGb3 complex and its cognate Vα14 T cell receptor suggest a model for dual recognition of foreign and self glycolipids
    • Zajonc D.M., Savage P.B., Bendelac A., Wilson I.A., and Teyton L. Crystal structures of mouse CD1d-iGb3 complex and its cognate Vα14 T cell receptor suggest a model for dual recognition of foreign and self glycolipids. J. Mol. Biol. 377 (2008) 1104-1116
    • (2008) J. Mol. Biol. , vol.377 , pp. 1104-1116
    • Zajonc, D.M.1    Savage, P.B.2    Bendelac, A.3    Wilson, I.A.4    Teyton, L.5
  • 14
  • 15
    • 6444240050 scopus 로고    scopus 로고
    • Effects of lipid chain lengths in α-galactosylceramides on cytokine release by natural killer T cells
    • Goff R.D., Gao Y., Mattner J., Zhou D., Yin N., Cantu III C., et al. Effects of lipid chain lengths in α-galactosylceramides on cytokine release by natural killer T cells. J. Am. Chem. Soc. 126 (2004) 13602-13603
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13602-13603
    • Goff, R.D.1    Gao, Y.2    Mattner, J.3    Zhou, D.4    Yin, N.5    Cantu III, C.6
  • 16
    • 33745884104 scopus 로고    scopus 로고
    • E and Z α-C-galactosylceramides by Julia-Lythgoe-Kocienski chemistry: a test of the receptor-binding model for glycolipid immunostimulants
    • Chen G., Chien M., Tsuji M., and Franck R.W. E and Z α-C-galactosylceramides by Julia-Lythgoe-Kocienski chemistry: a test of the receptor-binding model for glycolipid immunostimulants. ChemBioChem 7 (2006) 1017-1022
    • (2006) ChemBioChem , vol.7 , pp. 1017-1022
    • Chen, G.1    Chien, M.2    Tsuji, M.3    Franck, R.W.4
  • 17
    • 45549088950 scopus 로고    scopus 로고
    • Cutting edge: nonglycosidic CD1d lipid ligands activate human and murine invariant NKT cells
    • Silk J.D., Salio M., Reddy B.G., Shepherd D., Gileadi U., Brown J., et al. Cutting edge: nonglycosidic CD1d lipid ligands activate human and murine invariant NKT cells. J. Immunol. 180 (2008) 6452-6456
    • (2008) J. Immunol. , vol.180 , pp. 6452-6456
    • Silk, J.D.1    Salio, M.2    Reddy, B.G.3    Shepherd, D.4    Gileadi, U.5    Brown, J.6
  • 18
    • 33746042178 scopus 로고    scopus 로고
    • Structure-based discovery of glycolipids for CD1d-mediated NKT cell activation: tuning the adjuvant versus immunosuppression activity
    • Fujio M., Wu D., Garcia-Navarro R., Ho D.D., Tsuji M., and Wong C.-H. Structure-based discovery of glycolipids for CD1d-mediated NKT cell activation: tuning the adjuvant versus immunosuppression activity. J. Am. Chem. Soc. 128 (2006) 9022-9023
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9022-9023
    • Fujio, M.1    Wu, D.2    Garcia-Navarro, R.3    Ho, D.D.4    Tsuji, M.5    Wong, C.-H.6
  • 19
    • 51949119637 scopus 로고    scopus 로고
    • Quantitative microarray analysis of intact glycolipid-CD1d interaction and correlation with cell-based cytokine production
    • Liang P.-H., Imamura M., Li X., Wu D., Fujio M., Guy R.T., et al. Quantitative microarray analysis of intact glycolipid-CD1d interaction and correlation with cell-based cytokine production. J. Am. Chem. Soc. 130 (2008) 12348-12354
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12348-12354
    • Liang, P.-H.1    Imamura, M.2    Li, X.3    Wu, D.4    Fujio, M.5    Guy, R.T.6
  • 20
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding Y.H., Baker B.M., Garboczi D.N., Biddison W.E., and Wiley D.C. Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 11 (1999) 45-56
    • (1999) Immunity , vol.11 , pp. 45-56
    • Ding, Y.H.1    Baker, B.M.2    Garboczi, D.N.3    Biddison, W.E.4    Wiley, D.C.5
  • 21
    • 0033711639 scopus 로고    scopus 로고
    • Conservation of a T cell antagonist into an agonist by repairing a defect in the TCR/peptide/MHC interface: implications for TCR signaling
    • Baker B.M., Gagnon S.J., Biddison W.E., and Wiley D.C. Conservation of a T cell antagonist into an agonist by repairing a defect in the TCR/peptide/MHC interface: implications for TCR signaling. Immunity 13 (2000) 457-484
    • (2000) Immunity , vol.13 , pp. 457-484
    • Baker, B.M.1    Gagnon, S.J.2    Biddison, W.E.3    Wiley, D.C.4
  • 22
    • 42249107964 scopus 로고    scopus 로고
    • A minimal binding footprint on CD1d-glycolipid is a basis for selection of the unique human NKT TCR
    • Wun K.S., Borg N.A., Kjer-Nielsen L., Beddoe T., Koh R., Richardson S.K., et al. A minimal binding footprint on CD1d-glycolipid is a basis for selection of the unique human NKT TCR. J. Exp. Med. 205 (2008) 939-949
    • (2008) J. Exp. Med. , vol.205 , pp. 939-949
    • Wun, K.S.1    Borg, N.A.2    Kjer-Nielsen, L.3    Beddoe, T.4    Koh, R.5    Richardson, S.K.6
  • 25
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: looking beyond intuition
    • Müller K., Faeh C., and Diederich F. Fluorine in pharmaceuticals: looking beyond intuition. Science 317 (2007) 1881-1886
    • (2007) Science , vol.317 , pp. 1881-1886
    • Müller, K.1    Faeh, C.2    Diederich, F.3
  • 26
    • 34249054887 scopus 로고    scopus 로고
    • The length of lipids bound to human CD1d molecules modulates the affinity of NKT cell TCR and the threshold of NKT cell activation
    • McCarthy C., Shepherd D., Fleire S., Stronge V.S., Koch M., Illarionov P.A., et al. The length of lipids bound to human CD1d molecules modulates the affinity of NKT cell TCR and the threshold of NKT cell activation. J. Exp. Med. 204 (2007) 1131-1144
    • (2007) J. Exp. Med. , vol.204 , pp. 1131-1144
    • McCarthy, C.1    Shepherd, D.2    Fleire, S.3    Stronge, V.S.4    Koch, M.5    Illarionov, P.A.6
  • 27
    • 66949155720 scopus 로고    scopus 로고
    • Kinetics and cellular site of glycolipid loading control the outcome of natural killer T cell activation
    • Im J.S., Arora P., Bricard G., Molano A., Venkataswamy M.M., Baine I., et al. Kinetics and cellular site of glycolipid loading control the outcome of natural killer T cell activation. Immunity 30 (2009) 888-898
    • (2009) Immunity , vol.30 , pp. 888-898
    • Im, J.S.1    Arora, P.2    Bricard, G.3    Molano, A.4    Venkataswamy, M.M.5    Baine, I.6
  • 28
    • 2942739333 scopus 로고    scopus 로고
    • The clinical implication and molecular mechanism of preferential IL-4 production by modified glycolipid-stimulated NKT cells
    • Oki S., Chiba A., Yamamura T., and Miyake S. The clinical implication and molecular mechanism of preferential IL-4 production by modified glycolipid-stimulated NKT cells. J. Clin. Invest. 113 (2004) 1631-1640
    • (2004) J. Clin. Invest. , vol.113 , pp. 1631-1640
    • Oki, S.1    Chiba, A.2    Yamamura, T.3    Miyake, S.4
  • 30
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 31
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr., Sect. D: Biol. Crystallogr. 57 (2001) 1373-1382
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 34
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • Sheriff S., Hendrickson W.A., and Smith J.L. Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197 (1987) 273-296
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 35
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A32 (1976) 922-923
    • (1976) Acta Crystallogr. , vol.A32 , pp. 922-923
    • Kabsch, W.1
  • 36
    • 70350153643 scopus 로고    scopus 로고
    • Martin, A. C. R. & Porter, C. T. http://www.bioinf.org.uk/software/profit.
    • Martin, A. C. R. & Porter, C. T. http://www.bioinf.org.uk/software/profit.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.