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Volumn 8, Issue 1, 2012, Pages

The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; CHITIN; GBPA PROTEIN; GLYCAN; MUCIN; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; UNCLASSIFIED DRUG; CELL SURFACE RECEPTOR; COLONIZATION FACTOR ANTIGENS; FIMBRIA PROTEIN;

EID: 84857461967     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002373     Document Type: Article
Times cited : (142)

References (52)
  • 4
    • 33751368832 scopus 로고    scopus 로고
    • Editorial: A small step for WHO, a big step for cholera control
    • von Seidlein L, (2006) Editorial: A small step for WHO, a big step for cholera control. Trop Med Int Health 11: 1773-1774.
    • (2006) Trop Med Int Health , vol.11 , pp. 1773-1774
    • von Seidlein, L.1
  • 5
  • 6
    • 73949112064 scopus 로고    scopus 로고
    • High mortality in a cholera outbreak in western Kenya after post-election violence in 2008
    • Shikanga OT, Mutonga D, Abade M, Amwayi S, Ope M, et al. (2009) High mortality in a cholera outbreak in western Kenya after post-election violence in 2008. Am J Trop Med Hyg 81: 1085-1090.
    • (2009) Am J Trop Med Hyg , vol.81 , pp. 1085-1090
    • Shikanga, O.T.1    Mutonga, D.2    Abade, M.3    Amwayi, S.4    Ope, M.5
  • 7
    • 28644442881 scopus 로고    scopus 로고
    • A colonization factor links Vibrio cholerae environmental survival and human infection
    • Kirn TJ, Jude BA, Taylor RK, (2005) A colonization factor links Vibrio cholerae environmental survival and human infection. Nature 438: 863-866.
    • (2005) Nature , vol.438 , pp. 863-866
    • Kirn, T.J.1    Jude, B.A.2    Taylor, R.K.3
  • 9
    • 0021201015 scopus 로고
    • Influence of water temperature, salinity, and pH on survival and growth of toxigenic Vibrio cholerae serovar 01 associated with live copepods in laboratory microcosms
    • Huq A, West PA, Small EB, Huq MI, Colwell RR, (1984) Influence of water temperature, salinity, and pH on survival and growth of toxigenic Vibrio cholerae serovar 01 associated with live copepods in laboratory microcosms. Appl Environ Microbiol 48: 420-424.
    • (1984) Appl Environ Microbiol , vol.48 , pp. 420-424
    • Huq, A.1    West, P.A.2    Small, E.B.3    Huq, M.I.4    Colwell, R.R.5
  • 10
    • 14844297346 scopus 로고    scopus 로고
    • Vibrio cholerae persistence in aquatic environments and colonization of intestinal cells: involvement of a common adhesion mechanism
    • Zampini M, Pruzzo C, Bondre VP, Tarsi R, Cosmo M, et al. (2005) Vibrio cholerae persistence in aquatic environments and colonization of intestinal cells: involvement of a common adhesion mechanism. FEMS Microbiol Lett 244: 267-273.
    • (2005) FEMS Microbiol Lett , vol.244 , pp. 267-273
    • Zampini, M.1    Pruzzo, C.2    Bondre, V.P.3    Tarsi, R.4    Cosmo, M.5
  • 11
    • 0035403501 scopus 로고    scopus 로고
    • The mannose-sensitive hemagglutinin of Vibrio cholerae promotes adherence to zooplankton
    • Chiavelli DA, Marsh JW, Taylor RK, (2001) The mannose-sensitive hemagglutinin of Vibrio cholerae promotes adherence to zooplankton. Appl Environ Microbiol 67: 3220-3225.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3220-3225
    • Chiavelli, D.A.1    Marsh, J.W.2    Taylor, R.K.3
  • 12
    • 18244372943 scopus 로고    scopus 로고
    • Virulence and the environment: a novel role for Vibrio cholerae toxin-coregulated pili in biofilm formation on chitin
    • Reguera G, Kolter R, (2005) Virulence and the environment: a novel role for Vibrio cholerae toxin-coregulated pili in biofilm formation on chitin. J Bacteriol 187: 3551-3555.
    • (2005) J Bacteriol , vol.187 , pp. 3551-3555
    • Reguera, G.1    Kolter, R.2
  • 13
    • 55849092826 scopus 로고    scopus 로고
    • Intestinal adherence of Vibrio cholerae involves a coordinated interaction between colonization factor GbpA and mucin
    • Bhowmick R, Ghosal A, Das B, Koley H, Saha DR, et al. (2008) Intestinal adherence of Vibrio cholerae involves a coordinated interaction between colonization factor GbpA and mucin. Infect Immun 76: 4968-4977.
    • (2008) Infect Immun , vol.76 , pp. 4968-4977
    • Bhowmick, R.1    Ghosal, A.2    Das, B.3    Koley, H.4    Saha, D.R.5
  • 14
    • 73649139554 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation-putting the pieces together
    • Jensen PH, Kolarich D, Packer NH, (2010) Mucin-type O-glycosylation-putting the pieces together. FEBS J 277: 81-94.
    • (2010) FEBS J , vol.277 , pp. 81-94
    • Jensen, P.H.1    Kolarich, D.2    Packer, N.H.3
  • 15
    • 70349275888 scopus 로고    scopus 로고
    • Mass spectrometry in the analysis of N-linked and O-linked glycans
    • North SJ, Hitchen PG, Haslam SM, Dell A, (2009) Mass spectrometry in the analysis of N-linked and O-linked glycans. Curr Opin Struct Biol 19: 498-506.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 498-506
    • North, S.J.1    Hitchen, P.G.2    Haslam, S.M.3    Dell, A.4
  • 17
    • 0039391898 scopus 로고
    • Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin
    • Taylor RK, Miller VL, Furlong DB, Mekalanos JJ, (1987) Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin. Proc Natl Acad Sci U S A 84: 2833-2837.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 2833-2837
    • Taylor, R.K.1    Miller, V.L.2    Furlong, D.B.3    Mekalanos, J.J.4
  • 18
    • 17144462135 scopus 로고    scopus 로고
    • DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae
    • Heidelberg JF, Eisen JA, Nelson WC, Clayton RA, Gwinn ML, et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406: 477-483.
    • (2000) Nature , vol.406 , pp. 477-483
    • Heidelberg, J.F.1    Eisen, J.A.2    Nelson, W.C.3    Clayton, R.A.4    Gwinn, M.L.5
  • 20
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ, (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 382: 769-781.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 21
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad G, Horn SJ, van Aalten DM, Synstad B, Eijsink VG, (2005) The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 280: 28492-28497.
    • (2005) J Biol Chem , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    van Aalten, D.M.3    Synstad, B.4    Eijsink, V.G.5
  • 22
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, van Aalten DM, (2005) Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J Biol Chem 280: 11313-11319.
    • (2005) J Biol Chem , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.3    Eijsink, V.G.4    van Aalten, D.M.5
  • 23
    • 38849115087 scopus 로고    scopus 로고
    • Crystal structure of a novel bacterial cell-surface flagellin binding to a polysaccharide
    • Maruyama Y, Momma M, Mikami B, Hashimoto W, Murata K, (2008) Crystal structure of a novel bacterial cell-surface flagellin binding to a polysaccharide. Biochemistry 47: 1393-1402.
    • (2008) Biochemistry , vol.47 , pp. 1393-1402
    • Maruyama, Y.1    Momma, M.2    Mikami, B.3    Hashimoto, W.4    Murata, K.5
  • 25
    • 77952513211 scopus 로고    scopus 로고
    • Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting
    • Le Trong I, Aprikian P, Kidd BA, Forero-Shelton M, Tchesnokova V, et al. (2010) Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting. Cell 141: 645-655.
    • (2010) Cell , vol.141 , pp. 645-655
    • Le Trong, I.1    Aprikian, P.2    Kidd, B.A.3    Forero-Shelton, M.4    Tchesnokova, V.5
  • 26
    • 0033551911 scopus 로고    scopus 로고
    • X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli
    • Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, et al. (1999) X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science 285: 1061-1066.
    • (1999) Science , vol.285 , pp. 1061-1066
    • Choudhury, D.1    Thompson, A.2    Stojanoff, V.3    Langermann, S.4    Pinkner, J.5
  • 29
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D, Svergun DI, (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J Appl Crystallogr 42: 342-346.
    • (2009) J Appl Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 30
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI, (2003) Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 36: 860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 31
    • 10344233222 scopus 로고    scopus 로고
    • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
    • Blixt O, Head S, Mondala T, Scanlan C, Huflejt ME, et al. (2004) Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. Proc Natl Acad Sci U S A 101: 17033-17038.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17033-17038
    • Blixt, O.1    Head, S.2    Mondala, T.3    Scanlan, C.4    Huflejt, M.E.5
  • 32
    • 33750970829 scopus 로고    scopus 로고
    • Identification of ligand specificities for glycan-binding proteins using glycan arrays
    • Alvarez RA, Blixt O, (2006) Identification of ligand specificities for glycan-binding proteins using glycan arrays. Methods Enzymol 415: 292-310.
    • (2006) Methods Enzymol , vol.415 , pp. 292-310
    • Alvarez, R.A.1    Blixt, O.2
  • 35
    • 77949332482 scopus 로고    scopus 로고
    • Identification of novel contributions to high-affinity glycoprotein-receptor interactions using engineered ligands
    • Coombs PJ, Harrison R, Pemberton S, Quintero-Martinez A, Parry S, et al. (2010) Identification of novel contributions to high-affinity glycoprotein-receptor interactions using engineered ligands. J Mol Biol 396: 685-696.
    • (2010) J Mol Biol , vol.396 , pp. 685-696
    • Coombs, P.J.1    Harrison, R.2    Pemberton, S.3    Quintero-Martinez, A.4    Parry, S.5
  • 36
    • 45149112519 scopus 로고    scopus 로고
    • Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases
    • Glenn KA, Nelson RF, Wen HM, Mallinger AJ, Paulson HL, (2008) Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases. J Biol Chem 283: 12717-12729.
    • (2008) J Biol Chem , vol.283 , pp. 12717-12729
    • Glenn, K.A.1    Nelson, R.F.2    Wen, H.M.3    Mallinger, A.J.4    Paulson, H.L.5
  • 38
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution and density modification
    • Terwilliger TC, (2003) SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol 374: 22-37.
    • (2003) Methods Enzymol , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS, (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6: 458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 43
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI, (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89: 1237-1250.
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 44
    • 66349130414 scopus 로고    scopus 로고
    • Structural and functional characterization of a putative polysaccharide deacetylase of the human parasite Encephalitozoon cuniculi
    • Urch JE, Hurtado-Guerrero R, Brosson D, Liu Z, Eijsink VG, et al. (2009) Structural and functional characterization of a putative polysaccharide deacetylase of the human parasite Encephalitozoon cuniculi. Protein Sci 18: 1197-1209.
    • (2009) Protein Sci , vol.18 , pp. 1197-1209
    • Urch, J.E.1    Hurtado-Guerrero, R.2    Brosson, D.3    Liu, Z.4    Eijsink, V.G.5
  • 45
    • 0019427691 scopus 로고
    • Isolation and characterization of the native glycoprotein from pig small-intestinal mucus
    • Mantle M, Allen A, (1981) Isolation and characterization of the native glycoprotein from pig small-intestinal mucus. Biochem J 195: 267-275.
    • (1981) Biochem J , vol.195 , pp. 267-275
    • Mantle, M.1    Allen, A.2
  • 46
    • 0020075773 scopus 로고
    • In vitro adhesion of piliated Escherichia coli to small intestinal villous epithelial cells from rabbits and the identification of a soluble 987P pilus receptor-containing fraction
    • Dean EA, Isaacson RE, (1982) In vitro adhesion of piliated Escherichia coli to small intestinal villous epithelial cells from rabbits and the identification of a soluble 987P pilus receptor-containing fraction. Infect Immun 36: 1192-1198.
    • (1982) Infect Immun , vol.36 , pp. 1192-1198
    • Dean, E.A.1    Isaacson, R.E.2
  • 47
    • 0037064052 scopus 로고    scopus 로고
    • IKK beta and phosphatidylinositol 3-kinase/Akt participate in non-pathogenic Gram-negative enteric bacteria-induced RelA phosphorylation and NF-kappa B activation in both primary and intestinal epithelial cell lines
    • Haller D, Russo MP, Sartor RB, Jobin C, (2002) IKK beta and phosphatidylinositol 3-kinase/Akt participate in non-pathogenic Gram-negative enteric bacteria-induced RelA phosphorylation and NF-kappa B activation in both primary and intestinal epithelial cell lines. J Biol Chem 277: 38168-38178.
    • (2002) J Biol Chem , vol.277 , pp. 38168-38178
    • Haller, D.1    Russo, M.P.2    Sartor, R.B.3    Jobin, C.4
  • 48
    • 0029916571 scopus 로고    scopus 로고
    • Role of cell-associated N-acetyl-D-glucosamine specific haemagglutinin in the adhesion of Vibrio cholerae O1 to rabbit intestinal epithelial cells in vitro
    • Sasmal D, Guhathakurta B, Bhattacharya SK, Pal CR, Datta A, (1996) Role of cell-associated N-acetyl-D-glucosamine specific haemagglutinin in the adhesion of Vibrio cholerae O1 to rabbit intestinal epithelial cells in vitro. FEMS Immunol Med Microbiol 13: 101-105.
    • (1996) FEMS Immunol Med Microbiol , vol.13 , pp. 101-105
    • Sasmal, D.1    Guhathakurta, B.2    Bhattacharya, S.K.3    Pal, C.R.4    Datta, A.5
  • 49
    • 0015854977 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate
    • Filip C, Fletcher G, Wulff JL, Earhart CF, (1973) Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol 115: 717-722.
    • (1973) J Bacteriol , vol.115 , pp. 717-722
    • Filip, C.1    Fletcher, G.2    Wulff, J.L.3    Earhart, C.F.4
  • 50
    • 0037413885 scopus 로고    scopus 로고
    • Whole-bacterial cell enzyme-linked immunosorbent assay for cell-bound Moraxella bovis pili
    • Prieto CI, Rodriguez ME, Bosch A, Chirdo FG, Yantorno OM, (2003) Whole-bacterial cell enzyme-linked immunosorbent assay for cell-bound Moraxella bovis pili. Vet Microbiol 91: 157-168.
    • (2003) Vet Microbiol , vol.91 , pp. 157-168
    • Prieto, C.I.1    Rodriguez, M.E.2    Bosch, A.3    Chirdo, F.G.4    Yantorno, O.M.5
  • 51
    • 0017619349 scopus 로고
    • Intestinal fluid accumulation induced by oral challenge with Vibrio cholerae or cholera toxin in infant mice
    • Baselski V, Briggs R, Parker C, (1977) Intestinal fluid accumulation induced by oral challenge with Vibrio cholerae or cholera toxin in infant mice. Infect Immun 15: 704-712.
    • (1977) Infect Immun , vol.15 , pp. 704-712
    • Baselski, V.1    Briggs, R.2    Parker, C.3
  • 52
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: a sketchpad for protein structure topology cartoons
    • Bond CS, (2003) TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 19: 311-312.
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1


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