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Volumn 31, Issue 3, 2014, Pages 199-207

NMR study of short β(1-3)-glucans provides insights into the structure and interaction with Dectin-1

Author keywords

Dectin 1; DOSY; Isotope shift; STD NMR; glucan

Indexed keywords

BETA 1,3 GLUCAN; DECTIN 1; INTERLEUKIN 12; LAMINARAN; TUMOR NECROSIS FACTOR; BETA GLUCAN; DEUTERIUM; GLUCAN; LECTIN;

EID: 84897554674     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-013-9510-x     Document Type: Article
Times cited : (63)

References (45)
  • 1
    • 67649823470 scopus 로고    scopus 로고
    • β-glucan recognition by the innate immune system
    • Goodridge, H.S., Wolf, A.J., Underhill, D.M.: β-glucan recognition by the innate immune system. Immunol. Rev. 230, 38-50 (2009)
    • (2009) Immunol. Rev. , vol.230 , pp. 38-50
    • Goodridge, H.S.1    Wolf, A.J.2    Underhill, D.M.3
  • 2
    • 80051683071 scopus 로고    scopus 로고
    • Structural insights into recognition of triple-helical β-glucans by an insect fungal receptor
    • Kanagawa, M., Satoh, T., Ikeda, A., Adachi, Y., Ohno, N., Yamaguchi, Y.: Structural insights into recognition of triple-helical β-glucans by an insect fungal receptor. J. Biol. Chem. 286, 29158-29165 (2011)
    • (2011) J. Biol. Chem. , vol.286 , pp. 29158-29165
    • Kanagawa, M.1    Satoh, T.2    Ikeda, A.3    Adachi, Y.4    Ohno, N.5    Yamaguchi, Y.6
  • 3
    • 84872119020 scopus 로고    scopus 로고
    • An initial event in the insect innate immune response: Structural and biological studies of interactions between β-1,3-glucan and the N-terminal domain of β-1,3-glucan recognition protein
    • Dai, H., Hiromasa, Y., Takahashi, D., Vandervelde, D., Fabrick, J.A., Kanost, M.R., Krishnamoorthi, R.: An initial event in the insect innate immune response: structural and biological studies of interactions between β-1,3-glucan and the N-terminal domain of β-1,3-glucan recognition protein. Biochemistry 52, 161-170 (2013)
    • (2013) Biochemistry , vol.52 , pp. 161-170
    • Dai, H.1    Hiromasa, Y.2    Takahashi, D.3    Vandervelde, D.4    Fabrick, J.A.5    Kanost, M.R.6    Krishnamoorthi, R.7
  • 4
    • 12844253112 scopus 로고    scopus 로고
    • Family 6 carbohydrate binding modules recognize the non-reducing end of β-1,3-linked glucans by presenting a unique ligand binding surface
    • van Bueren, A.L., Morland, C., Gilbert, H.J., Boraston, A.B.: Family 6 carbohydrate binding modules recognize the non-reducing end of β-1,3-linked glucans by presenting a unique ligand binding surface. J. Biol. Chem. 280, 530-537 (2005)
    • (2005) J. Biol. Chem. , vol.280 , pp. 530-537
    • Van Bueren, A.L.1    Morland, C.2    Gilbert, H.J.3    Boraston, A.B.4
  • 5
    • 0035817818 scopus 로고    scopus 로고
    • Immune recognition. A new receptor for β-glucans
    • Brown, G.D., Gordon, S.: Immune recognition. A new receptor for β-glucans. Nature 413, 36-37 (2001)
    • (2001) Nature , vol.413 , pp. 36-37
    • Brown, G.D.1    Gordon, S.2
  • 9
    • 84861578183 scopus 로고    scopus 로고
    • Synthesis of β(1,3) oligoglucans exhibiting a Dectin-1 binding affinity and their biological evaluation
    • Tanaka, H., Kawai, T., Adachi, Y., Hanashima, S., Yamaguchi, Y., Ohno, N., Takahashi, T.: Synthesis of β(1,3) oligoglucans exhibiting a Dectin-1 binding affinity and their biological evaluation. Bioorg. Med. Chem. 20, 3898-3914 (2012)
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 3898-3914
    • Tanaka, H.1    Kawai, T.2    Adachi, Y.3    Hanashima, S.4    Yamaguchi, Y.5    Ohno, N.6    Takahashi, T.7
  • 11
    • 33244497571 scopus 로고    scopus 로고
    • Dectin-1: A signalling non-TLR pattern-recognition receptor
    • Brown, G.D.: Dectin-1: a signalling non-TLR pattern-recognition receptor. Nat. Rev. Immunol. 6, 33-43 (2006)
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 33-43
    • Brown, G.D.1
  • 13
    • 77958506282 scopus 로고    scopus 로고
    • β(1,3) Branched heptadeca- and linear hexadeca-saccharides possessing an aminoalkyl group as a strong ligand to dectin-1
    • Camb.
    • Tanaka, H., Kawai, T., Adachi, Y., Ohno, N., Takahashi, T.: β(1,3) Branched heptadeca- and linear hexadeca-saccharides possessing an aminoalkyl group as a strong ligand to dectin-1. Chem. Commun. (Camb.) 46, 8249-8251 (2010)
    • (2010) Chem. Commun. , vol.46 , pp. 8249-8251
    • Tanaka, H.1    Kawai, T.2    Adachi, Y.3    Ohno, N.4    Takahashi, T.5
  • 14
    • 0000546271 scopus 로고
    • The triple helical structure of lentinan, a linear β-(1→3)-D- glucan
    • Bluhm, T.L., Sarko, A.: The triple helical structure of lentinan, a linear β-(1→3)-D-glucan. Can. J. Chem. 55, 293-299 (1977)
    • (1977) Can. J. Chem. , vol.55 , pp. 293-299
    • Bluhm, T.L.1    Sarko, A.2
  • 15
    • 33845550524 scopus 로고
    • Packing analysis of carbohydrates and polysaccharides.14. Triple-helical crystalline-structure of curdlan and paramylon hydrates
    • Chuah, C.T., Sarko, A., Deslandes, Y., Marchessault, R.H.: Packing analysis of carbohydrates and polysaccharides.14. Triple-helical crystalline-structure of curdlan and paramylon hydrates. Macromolecules 16, 1375-1382 (1983)
    • (1983) Macromolecules , vol.16 , pp. 1375-1382
    • Chuah, C.T.1    Sarko, A.2    Deslandes, Y.3    Marchessault, R.H.4
  • 16
    • 0026663427 scopus 로고
    • Conformation-dependent change in antitumor activity of linear and branched (1 → 3)-β-D-glucans on the basis of conformational elucidation by carbon-13 nuclear magnetic resonance spectroscopy
    • Yoshioka, Y., Uehara, N., Saito, H.: Conformation-dependent change in antitumor activity of linear and branched (1 → 3)-β-D-glucans on the basis of conformational elucidation by carbon-13 nuclear magnetic resonance spectroscopy. Chem. Pharm. Bull. 40, 1221-1226 (1992)
    • (1992) Chem. Pharm. Bull. , vol.40 , pp. 1221-1226
    • Yoshioka, Y.1    Uehara, N.2    Saito, H.3
  • 17
    • 0031014343 scopus 로고    scopus 로고
    • Correlation between immunological activity, molar mass, and molecular structure of different (1→3)-β-D-glucans
    • Kulicke, W.M., Lettau, A.I., Thielking, H.: Correlation between immunological activity, molar mass, and molecular structure of different (1→3)-β-D-glucans. Carbohydr. Res. 297, 135-143 (1997)
    • (1997) Carbohydr. Res. , vol.297 , pp. 135-143
    • Kulicke, W.M.1    Lettau, A.I.2    Thielking, H.3
  • 18
    • 0034697013 scopus 로고    scopus 로고
    • Observation of a partially opened triple-helix conformation in 1->3-β-glucan by fluorescence resonance energy transfer spectroscopy
    • Young, S.H., Dong, W.J., Jacobs, R.R.: Observation of a partially opened triple-helix conformation in 1->3-β-glucan by fluorescence resonance energy transfer spectroscopy. J. Biol. Chem. 275, 11874-11879 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 11874-11879
    • Young, S.H.1    Dong, W.J.2    Jacobs, R.R.3
  • 20
    • 25444438763 scopus 로고    scopus 로고
    • β-1,3-glucan polysaccharides as novel one-dimensional hosts for DNA/RNA, conjugated polymers and nanoparticles
    • Camb
    • Sakurai, K., Uezu, K., Numata, M., Hasegawa, T., Li, C., Kaneko, K., Shinkai, S.: β-1,3-glucan polysaccharides as novel one-dimensional hosts for DNA/RNA, conjugated polymers and nanoparticles. Chem. Commun. (Camb), 4383-4398 (2005)
    • (2005) Chem. Commun. , pp. 4383-4398
    • Sakurai, K.1    Uezu, K.2    Numata, M.3    Hasegawa, T.4    Li, C.5    Kaneko, K.6    Shinkai, S.7
  • 21
    • 42949162957 scopus 로고    scopus 로고
    • Higher order structure of (1,3)-β-Dglucans and its influence on their biological activities and complexation abilities
    • Sletmoen, M., Stokke, B.T.: Higher order structure of (1,3)-β-Dglucans and its influence on their biological activities and complexation abilities. Biopolymers 89, 310-321 (2008)
    • (2008) Biopolymers , vol.89 , pp. 310-321
    • Sletmoen, M.1    Stokke, B.T.2
  • 22
    • 24344466934 scopus 로고    scopus 로고
    • Carbon-13 NMR method for the detection of correlated hydrogen exchange at adjacent back-bone peptide amides and its application to hydrogen exchange in five antiparallel β strands within the hydrophobic core of Streptomyces subtilisin inhibitor (SSI)
    • Uchida, K., Markley, J.L., Kainosho, M.: Carbon-13 NMR method for the detection of correlated hydrogen exchange at adjacent back-bone peptide amides and its application to hydrogen exchange in five antiparallel β strands within the hydrophobic core of Streptomyces subtilisin inhibitor (SSI). Biochemistry 44, 11811-11820 (2005)
    • (2005) Biochemistry , vol.44 , pp. 11811-11820
    • Uchida, K.1    Markley, J.L.2    Kainosho, M.3
  • 23
    • 80052932950 scopus 로고    scopus 로고
    • 13C-NMR quantification of proton exchange at LewisX hydroxyl groups in water
    • Camb.
    • 13C-NMR quantification of proton exchange at LewisX hydroxyl groups in water. Chem. Commun. (Camb.) 47, 10800-10802 (2011)
    • (2011) Chem. Commun. , vol.47 , pp. 10800-10802
    • Hanashima, S.1    Kato, K.2    Yamaguchi, Y.3
  • 24
    • 0347359145 scopus 로고    scopus 로고
    • Diffusion ordered nuclear magnetic resonance spectroscopy: Principles and applications
    • Johnson, C.S.: Diffusion ordered nuclear magnetic resonance spectroscopy: principles and applications. Prog. NMR Spect. 34, 203-256 (1999)
    • (1999) Prog. NMR Spect. , vol.34 , pp. 203-256
    • Johnson, C.S.1
  • 25
    • 0034693205 scopus 로고    scopus 로고
    • Studies of the complexation of sugars by diffusion-ordered NMR spectroscopy
    • Díaz, M.D., Berger, S.: Studies of the complexation of sugars by diffusion-ordered NMR spectroscopy. Carbohydr. Res. 329, 1-5 (2000)
    • (2000) Carbohydr. Res. , vol.329 , pp. 1-5
    • Díaz, M.D.1    Berger, S.2
  • 27
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer, M., Meyer, B.: Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 123, 6108-6117 (2001)
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 28
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M., Meyer, B.: Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 38, 1784-1788 (1999)
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 29
    • 10944256235 scopus 로고    scopus 로고
    • Competition STD NMR for the detection of high-affinity ligands and NMR-based screening
    • Wang, Y.S., Liu, D., Wyss, D.F.: Competition STD NMR for the detection of high-affinity ligands and NMR-based screening. Magn. Reson. Chem. 42, 485-489 (2004)
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 485-489
    • Wang, Y.S.1    Liu, D.2    Wyss, D.F.3
  • 31
    • 44949277996 scopus 로고
    • A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents
    • Gibbs, S.J., Johnson, C.S.: A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents. J. Magn. Reson. 93, 395-402 (1991)
    • (1991) J. Magn. Reson. , vol.93 , pp. 395-402
    • Gibbs, S.J.1    Johnson, C.S.2
  • 34
    • 0029920166 scopus 로고    scopus 로고
    • Hydrogen/deuterium isotope effects on the NMR chemical shifts and geometries of intermolecular low-barrier hydrogen-bonded complexes
    • Smirnov, S.N., Golubev, N.S., Denisov, G.S., Benedict, H., SchahMohammedi, P., Limbach, H.H.: Hydrogen/deuterium isotope effects on the NMR chemical shifts and geometries of intermolecular low-barrier hydrogen-bonded complexes. J. Am. Chem. Soc. 118, 4094-4101 (1996)
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4094-4101
    • Smirnov, S.N.1    Golubev, N.S.2    Denisov, G.S.3    Benedict, H.4    SchahMohammedi, P.5    Limbach, H.H.6
  • 35
    • 84945629805 scopus 로고
    • 2 due to zero-point vibration
    • 2 due to zero-point vibration. Mol. Phys. 4, 61-63 (1961)
    • (1961) Mol. Phys. , vol.4 , pp. 61-63
    • Marshall, T.W.1
  • 36
    • 0030060928 scopus 로고    scopus 로고
    • Analysis of the structural heterogeneity of laminarin by electrospray-ionisation-mass spectrometry
    • Read, S.M., Currie, G., Bacic, A.: Analysis of the structural heterogeneity of laminarin by electrospray-ionisation-mass spectrometry. Carbohydr. Res. 281, 187-201 (1996)
    • (1996) Carbohydr. Res. , vol.281 , pp. 187-201
    • Read, S.M.1    Currie, G.2    Bacic, A.3
  • 37
    • 0011887937 scopus 로고
    • Determination of molecular-weight distributions for polymers by diffusion-ordered NMR
    • Chen, A., Wu, D.H., Johnson, C.S.: Determination of molecular-weight distributions for polymers by diffusion-ordered NMR. J. Am. Chem. Soc. 117, 7965-7970 (1995)
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7965-7970
    • Chen, A.1    Wu, D.H.2    Johnson, C.S.3
  • 38
    • 33748427533 scopus 로고    scopus 로고
    • Immunostimulatory polysaccharides from Chlorella pyrenoidosa. A new galactofuranan. Measurement of molecular weight and molecular weight dispersion by DOSY NMR
    • Suárez, E.R., Syvitski, R., Kralovec, J.A., Noseda, M.D., Barrow, C.J., Ewart, H.S., Lumsden, M.D., Grindley, T.B.: Immunostimulatory polysaccharides from Chlorella pyrenoidosa. A new galactofuranan. measurement of molecular weight and molecular weight dispersion by DOSY NMR. Biomacromolecules 7, 2368-2376 (2006)
    • (2006) Biomacromolecules , vol.7 , pp. 2368-2376
    • Suárez, E.R.1    Syvitski, R.2    Kralovec, J.A.3    Noseda, M.D.4    Barrow, C.J.5    Ewart, H.S.6    Lumsden, M.D.7    Grindley, T.B.8
  • 39
  • 40
    • 84981408535 scopus 로고
    • Some aspects of stereochemistry and hydrogen bonding of carbohydrate related to polysaccharide conformations
    • Sundaralingam, M.: Some aspects of stereochemistry and hydrogen bonding of carbohydrate related to polysaccharide conformations. Biopolymers 6, 189-213 (1968)
    • (1968) Biopolymers , vol.6 , pp. 189-213
    • Sundaralingam, M.1
  • 41
    • 0012824174 scopus 로고
    • Crystal and molecular-structure of a 3:2 mixture of laminarabiose and O-α-D-glucopyranosyl-(1→3)-β-D-glucopyranose
    • Takeda, H., Yasuoka, N., Kasai, N.: Crystal and molecular-structure of a 3:2 mixture of laminarabiose and O-α-D-glucopyranosyl-(1→3)-β-D- glucopyranose. Carbohydr. Res. 53, 137-152 (1977)
    • (1977) Carbohydr. Res. , vol.53 , pp. 137-152
    • Takeda, H.1    Yasuoka, N.2    Kasai, N.3
  • 42
    • 0027086959 scopus 로고
    • Crystal structure of methyl 3-O-β-D-glucopyranosyl-β-D- glucopyranoside (methyl β-D-laminarabioside) monohydrate
    • Noguchi, K., Okuyama, K., Kitamura, S., Takeo, K.: Crystal structure of methyl 3-O-β-D-glucopyranosyl-β-D-glucopyranoside (methyl β-D-laminarabioside) monohydrate. Carbohydr. Res. 237, 33-43 (1992)
    • (1992) Carbohydr. Res. , vol.237 , pp. 33-43
    • Noguchi, K.1    Okuyama, K.2    Kitamura, S.3    Takeo, K.4
  • 43
    • 46449115657 scopus 로고    scopus 로고
    • 13C-labeled glucobiosides using inter-residue scalar coupling constants
    • 13C-labeled glucobiosides using inter-residue scalar coupling constants. J. Phys. Chem. B 112, 4447-4453 (2008)
    • (2008) J. Phys. Chem. B , vol.112 , pp. 4447-4453
    • Olsson, U.1    Serianni, A.S.2    Stenutz, R.3
  • 44
    • 0344513901 scopus 로고    scopus 로고
    • Diffusion-ordered NMR spectroscopy: A versatile tool for the molecular weight determination of uncharged polysaccharides
    • Viel, S., Capitani, D., Mannina, L., Segre, A.: Diffusion-ordered NMR spectroscopy: A versatile tool for the molecular weight determination of uncharged polysaccharides. Biomacromolecules 4, 1843-1847 (2003)
    • (2003) Biomacromolecules , vol.4 , pp. 1843-1847
    • Viel, S.1    Capitani, D.2    Mannina, L.3    Segre, A.4
  • 45
    • 0000233598 scopus 로고
    • Static and dynamic solution properties of pullulan in a dilute-solution
    • Kato, T., Katsuki, T., Takahashi, A.: Static and dynamic solution properties of pullulan in a dilute-solution. Macromolecules 17, 1726-1730 (1984)
    • (1984) Macromolecules , vol.17 , pp. 1726-1730
    • Kato, T.1    Katsuki, T.2    Takahashi, A.3


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