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Volumn 31, Issue 1, 2014, Pages 7-12

Human tandem-repeat-type galectins bind bacterial non-βGal polysaccharides

Author keywords

ABO; Bacterial polysaccharide; Galectin; Glycan; Printed glycan array; Rhamnoside

Indexed keywords

BACTERIAL POLYSACCHARIDE; BETA GALACTOSIDASE; ECALECTIN; GALACTOSE; GALECTIN 4; GALECTIN 8;

EID: 84893345841     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-013-9497-3     Document Type: Article
Times cited : (35)

References (32)
  • 2
    • 79958036381 scopus 로고    scopus 로고
    • From lectin structure to functional glycomics: Principles of the sugar code
    • 1:CAS:528:DC%2BC3MXnsVOqs7w%3D 21458998 10.1016/j.tibs.2011.01.005
    • Gabius, H.-J., André, S., Jiménez-Barbero, J., Romero, A., Solís, D.: From lectin structure to functional glycomics: principles of the sugar code. Trends Biochem. Sci. 36, 298-313 (2011)
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 298-313
    • Gabius, H.-J.1    André, S.2    Jiménez-Barbero, J.3    Romero, A.4    Solís, D.5
  • 3
    • 15944390196 scopus 로고    scopus 로고
    • How C-type lectins detect pathogens
    • 1:CAS:528:DC%2BD2MXjtVCjt7s%3D 15760448 10.1111/j.1462-5822.2005.00506.x
    • Cambi, A., Koopman, M., Figdor, C.G.: How C-type lectins detect pathogens. Cell. Microbiol. 7, 481-488 (2005)
    • (2005) Cell. Microbiol. , vol.7 , pp. 481-488
    • Cambi, A.1    Koopman, M.2    Figdor, C.G.3
  • 4
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • 1:CAS:528:DC%2BD1MXlvFSiu7g%3D 3759161 19444247 10.1038/nrmicro2146
    • Vasta, G.R.: Roles of galectins in infection. Nat. Rev. Microbiol. 7, 424-438 (2009)
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 5
    • 0030049078 scopus 로고    scopus 로고
    • The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites
    • 1:CAS:528:DyaK28XpvVWquw%3D%3D 8568262
    • Mey, A., Leffler, H., Hmama, Z., Normier, G., Revillard, J.-P.: The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites. J. Immunol. 156, 1572-1577 (1996)
    • (1996) J. Immunol. , vol.156 , pp. 1572-1577
    • Mey, A.1    Leffler, H.2    Hmama, Z.3    Normier, G.4    Revillard, J.-P.5
  • 6
    • 33749125248 scopus 로고    scopus 로고
    • Galectin-3 induces death of Candida species expressing specific β1,2-linked mannans
    • 1:CAS:528:DC%2BD28Xps1Gnsrg%3D 16982911
    • Kohatsu, L., Hsu, D.K., Jegalian, A.G., Liu, F.-T., Baum, L.G.: Galectin-3 induces death of Candida species expressing specific β1,2-linked mannans. J. Immunol. 177, 4718-4726 (2006)
    • (2006) J. Immunol. , vol.177 , pp. 4718-4726
    • Kohatsu, L.1    Hsu, D.K.2    Jegalian, A.G.3    Liu, F.-T.4    Baum, L.G.5
  • 7
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • 1:CAS:528:DC%2BD38XmvVagsL4%3D 12223271 10.1016/S0304-4165(02)00310-0
    • Cooper, D.N.W.: Galectinomics: finding themes in complexity. Biochim. Biophys. Acta 1572, 209-231 (2002)
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 8
    • 84857738686 scopus 로고    scopus 로고
    • A toolbox of lectins for translating the sugar code: The galectin network in phylogenesis and tumors
    • 1:CAS:528:DC%2BC38XosFSiurc%3D 22374719
    • Kaltner, H., Gabius, H.-J.: A toolbox of lectins for translating the sugar code: the galectin network in phylogenesis and tumors. Histol. Histopathol. 27, 397-416 (2012)
    • (2012) Histol. Histopathol. , vol.27 , pp. 397-416
    • Kaltner, H.1    Gabius, H.-J.2
  • 10
    • 52249120592 scopus 로고    scopus 로고
    • Statistical analysis of the Bacterial Carbohydrate Structure Data Base (BCSDB): Characteristics and diversity of bacterial carbohydrates in comparison with mammalian glycans
    • 2543016 18694500 10.1186/1472-6807-8-35
    • Herget, S., Toukach, P.V., Ranzinger, R., Hull, W.E., Knirel, Y.A., von der Lieth, C.-W.: Statistical analysis of the Bacterial Carbohydrate Structure Data Base (BCSDB): characteristics and diversity of bacterial carbohydrates in comparison with mammalian glycans. BMC Struct. Biol. 8, 35 (2008)
    • (2008) BMC Struct. Biol. , vol.8 , pp. 35
    • Herget, S.1    Toukach, P.V.2    Ranzinger, R.3    Hull, W.E.4    Knirel, Y.A.5    Von Der Lieth, C.-W.6
  • 11
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain
    • 1:CAS:528:DyaK3sXisFSjt7c%3D 8449956
    • Oda, Y., Herrmann, J., Gitt, M.A., Turck, C.W., Burlingame, A.L., Barondes, S.H., Leffler, H.: Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain. J. Biol. Chem. 268, 5929-5939 (1993)
    • (1993) J. Biol. Chem. , vol.268 , pp. 5929-5939
    • Oda, Y.1    Herrmann, J.2    Gitt, M.A.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, S.H.6    Leffler, H.7
  • 13
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galβ1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • 1:CAS:528:DC%2BD2cXkvVKlt7s%3D 15194236 10.1016/j.biochi.2004.03.007
    • Wu, A.M., Wu, J.H., Liu, J.-H., Singh, T., André, S., Kaltner, H., Gabius, H.-J.: Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galβ1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochimie 86, 317-326 (2004)
    • (2004) Biochimie , vol.86 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4    André, S.5    Kaltner, H.6    Gabius, H.-J.7
  • 14
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • 1:CAS:528:DC%2BD2MXhtVymtrg%3D 15546874 10.1074/jbc.M410362200
    • Ideo, H., Seko, A., Yamashita, K.: Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J. Biol. Chem. 280, 4730-4737 (2005)
    • (2005) J. Biol. Chem. , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 15
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain
    • 1:CAS:528:DC%2BD1cXotlOhs70%3D 18456665 10.1074/jbc.M802495200
    • Stowell, S.R., Arthur, C.M., Slanina, K.A., Horton, J.R., Smith, D.F., Cummings, R.D.: Dimeric Galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the C-terminal domain. J. Biol. Chem. 283, 20547-20559 (2008)
    • (2008) J. Biol. Chem. , vol.283 , pp. 20547-20559
    • Stowell, S.R.1    Arthur, C.M.2    Slanina, K.A.3    Horton, J.R.4    Smith, D.F.5    Cummings, R.D.6
  • 16
    • 41549129317 scopus 로고    scopus 로고
    • Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: A case study on galectins-1 and -3 and the impact of assay setting
    • 1:CAS:528:DC%2BD1cXltlektrc%3D 18256179 10.1093/glycob/cwn009
    • Rapoport, E.M., André, S., Kurmyshkina, O.V., Pochechueva, T.V., Severov, V.V., Pazynina, G.V., Gabius, H.-J., Bovin, N.V.: Galectin-loaded cells as a platform for the profiling of lectin specificity by fluorescent neoglycoconjugates: a case study on galectins-1 and -3 and the impact of assay setting. Glycobiology 18, 315-324 (2008)
    • (2008) Glycobiology , vol.18 , pp. 315-324
    • Rapoport, E.M.1    André, S.2    Kurmyshkina, O.V.3    Pochechueva, T.V.4    Severov, V.V.5    Pazynina, G.V.6    Gabius, H.-J.7    Bovin, N.V.8
  • 19
    • 78649773993 scopus 로고    scopus 로고
    • Human galectin-3 (Mac-2 antigen): Defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region
    • 1:CAS:528:DC%2BC3cXhs1ajsL7O 21070836 10.1016/j.bbagen.2010.11.001
    • Krzeminski, M., Singh, T., André, S., Lensch, M., Wu, A.M., Bonvin, A.M.J.J., Gabius, H.-J.: Human galectin-3 (Mac-2 antigen): defining molecular switches of affinity to natural glycoproteins, structural and dynamic aspects of glycan binding by flexible ligand docking and putative regulatory sequences in the proximal promoter region. Biochim. Biophys. Acta 1810, 150-161 (2011)
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 150-161
    • Krzeminski, M.1    Singh, T.2    André, S.3    Lensch, M.4    Wu, A.M.5    Bonvin, A.6    Gabius, H.-J.7
  • 20
    • 84876782219 scopus 로고    scopus 로고
    • The third dimension of reading the sugar code by lectins: Design of glycoclusters with cyclic scaffolds as tools with the aim to define correlations between spatial presentation and activity
    • 1:CAS:528:DC%2BC3sXmt1Glt7Y%3D 23558543 10.3390/molecules18044026
    • Murphy, P.V., André, S., Gabius, H.-J.: The third dimension of reading the sugar code by lectins: design of glycoclusters with cyclic scaffolds as tools with the aim to define correlations between spatial presentation and activity. Molecules 18, 4026-4053 (2013)
    • (2013) Molecules , vol.18 , pp. 4026-4053
    • Murphy, P.V.1    André, S.2    Gabius, H.-J.3
  • 22
    • 0025076613 scopus 로고
    • Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands
    • 1:CAS:528:DyaK3MXivVCl 2278395 10.1016/0003-2697(90)90050-J
    • Gabius, H.-J.: Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands. Anal. Biochem. 189, 91-94 (1990)
    • (1990) Anal. Biochem. , vol.189 , pp. 91-94
    • Gabius, H.-J.1
  • 24
    • 0026093104 scopus 로고
    • Lectin localization in human nerve by biochemically defined lectin-binding glycoproteins, neoglycoprotein and lectin-specific antibody
    • 1:CAS:528:DyaK3MXhvVWmsLY%3D 2050547 10.1007/BF00266777
    • Gabius, H.-J., Wosgien, B., Hendrys, M., Bardosi, A.: Lectin localization in human nerve by biochemically defined lectin-binding glycoproteins, neoglycoprotein and lectin-specific antibody. Histochemistry 95, 269-277 (1991)
    • (1991) Histochemistry , vol.95 , pp. 269-277
    • Gabius, H.-J.1    Wosgien, B.2    Hendrys, M.3    Bardosi, A.4
  • 25
    • 84655170133 scopus 로고    scopus 로고
    • Synthesis of bivalent lactosides and their activity as sensors for differences between lectins in inter- and intrafamily comparisons
    • 22142540 10.1016/j.bmcl.2011.11.010
    • André, S., Jarikote, D.V., Yan, D., Vincenz, L., Wang, G.N., Kaltner, H., Murphy, P.V., Gabius, H.-J.: Synthesis of bivalent lactosides and their activity as sensors for differences between lectins in inter- and intrafamily comparisons. Bioorg. Med. Chem. Lett. 22, 313-318 (2012)
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 313-318
    • André, S.1    Jarikote, D.V.2    Yan, D.3    Vincenz, L.4    Wang, G.N.5    Kaltner, H.6    Murphy, P.V.7    Gabius, H.-J.8
  • 26
    • 84867580385 scopus 로고    scopus 로고
    • INK4a: Anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model
    • 1:CAS:528:DC%2BC38XhsFSgsb%2FO 22943525 10.1111/febs.12001
    • INK4a: anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model. FEBS J. 279, 4062-4080 (2012)
    • (2012) FEBS J. , vol.279 , pp. 4062-4080
    • Amano, M.1    Eriksson, H.2    Manning, J.C.3    Detjen, K.M.4    André, S.5    Nishimura, S.-I.6    Lehtiö, J.7    Gabius, H.-J.8
  • 27
    • 0002447206 scopus 로고
    • Bacterial lipopolysaccharides. Extraction with phenol-water and further applications of the procedure
    • 1:CAS:528:DyaF2MXktFSgtLY%3D
    • Westphal, O., Jann, K.: Bacterial lipopolysaccharides. Extraction with phenol-water and further applications of the procedure. Methods Carbohydr. Chem. 5, 83-91 (1965)
    • (1965) Methods Carbohydr. Chem. , vol.5 , pp. 83-91
    • Westphal, O.1    Jann, K.2
  • 28
    • 77956397832 scopus 로고    scopus 로고
    • Structure of the O-polysaccharide of Cronobacter sakazakii O2 with a randomly O-acetylated l-rhamnose residue
    • 1:CAS:528:DC%2BC3cXhtFaiurbL 20692652 10.1016/j.carres.2010.07.014
    • Arbatsky, N.P., Wang, M., Shashkov, A.S., Chizhov, A.O., Feng, L., Knirel, Y.A., Wang, L.: Structure of the O-polysaccharide of Cronobacter sakazakii O2 with a randomly O-acetylated l-rhamnose residue. Carbohydr. Res. 345, 2090-2094 (2010)
    • (2010) Carbohydr. Res. , vol.345 , pp. 2090-2094
    • Arbatsky, N.P.1    Wang, M.2    Shashkov, A.S.3    Chizhov, A.O.4    Feng, L.5    Knirel, Y.A.6    Wang, L.7
  • 30
    • 79960243415 scopus 로고    scopus 로고
    • Galectins as tools for glycan mapping in histology: Comparison of their binding profiles to the bovine zona pellucida by confocal laser scanning microscopy
    • 1:CAS:528:DC%2BC3MXmvVKgtrw%3D 21584695 10.1007/s00418-011-0814-2
    • Habermann, F.A., André, S., Kaltner, H., Kübler, D., Sinowatz, F., Gabius, H.-J.: Galectins as tools for glycan mapping in histology: comparison of their binding profiles to the bovine zona pellucida by confocal laser scanning microscopy. Histochem. Cell Biol. 135, 539-552 (2011)
    • (2011) Histochem. Cell Biol. , vol.135 , pp. 539-552
    • Habermann, F.A.1    André, S.2    Kaltner, H.3    Kübler, D.4    Sinowatz, F.5    Gabius, H.-J.6
  • 31
    • 84866366641 scopus 로고    scopus 로고
    • Adhesion/growth-regulatory galectins in the human eye: Localization profiles and tissue reactivities as a standard to detect disease-associated alterations
    • 22527325 10.1007/s00417-012-2021-9
    • Schlötzer-Schrehardt, U., Andre, S., Janko, C., Kaltner, H., Kopitz, J., Gabius, H.J., Herrmann, M.: Adhesion/growth-regulatory galectins in the human eye: localization profiles and tissue reactivities as a standard to detect disease-associated alterations. Graefes Arch. Clin. Exp. Ophthalmol. 250, 1169-1180 (2012)
    • (2012) Graefes Arch. Clin. Exp. Ophthalmol. , vol.250 , pp. 1169-1180
    • Schlötzer-Schrehardt, U.1    Andre, S.2    Janko, C.3    Kaltner, H.4    Kopitz, J.5    Gabius, H.J.6    Herrmann, M.7
  • 32
    • 0020584499 scopus 로고
    • Membrane glycoproteins glycolipids and membrane lectins as recognition signals in normal and malignant cells
    • 1:CAS:528:DyaL3sXktVelsL8%3D
    • Monsigny, M., Kieda, C., Roche, A.-C.: Membrane glycoproteins glycolipids and membrane lectins as recognition signals in normal and malignant cells. Biol. Cell 47, 95-110 (1983)
    • (1983) Biol. Cell , vol.47 , pp. 95-110
    • Monsigny, M.1    Kieda, C.2    Roche, A.-C.3


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