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Volumn 195, Issue 14, 2013, Pages 3277-3286

Structural basis for biofilm formation via the Vibrio cholerae matrix protein RbmA

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; PROTEIN RBMA; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

EID: 84880030391     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00374-13     Document Type: Article
Times cited : (57)

References (48)
  • 1
    • 61449151985 scopus 로고    scopus 로고
    • Vibrio biofilms: so much the same yet so different
    • Yildiz FH, Visick KL. 2009. Vibrio biofilms: so much the same yet so different. Trends Microbiol. 17:109-118.
    • (2009) Trends Microbiol. , vol.17 , pp. 109-118
    • Yildiz, F.H.1    Visick, K.L.2
  • 2
    • 0242523776 scopus 로고    scopus 로고
    • Bacterial biofilms: an emerging link to disease pathogenesis
    • Parsek MR, Singh PK. 2003. Bacterial biofilms: an emerging link to disease pathogenesis. Annu. Rev. Microbiol. 57:677-701.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 677-701
    • Parsek, M.R.1    Singh, P.K.2
  • 7
    • 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
    • 0029937317 scopus 로고    scopus 로고
    • A simple filtration method to remove plankton-associated Vibrio cholerae in raw water supplies in developing countries
    • Huq A, Xu B, Chowdhury MA, Islam MS, Montilla R, Colwell RR. 1996. A simple filtration method to remove plankton-associated Vibrio cholerae in raw water supplies in developing countries. Appl. Environ. Microbiol. 62:2508-2512.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2508-2512
    • Huq, A.1    Xu, B.2    Chowdhury, M.A.3    Islam, M.S.4    Montilla, R.5    Colwell, R.R.6
  • 12
    • 77956366219 scopus 로고    scopus 로고
    • Role of Vibrio polysaccharide (vps) genes in VPS production, biofilm formation and Vibrio cholerae pathogenesis
    • Fong JC, Syed KA, Klose KE, Yildiz FH. 2010. Role of Vibrio polysaccharide (vps) genes in VPS production, biofilm formation and Vibrio cholerae pathogenesis. Microbiology 156:2757-2769.
    • (2010) Microbiology , vol.156 , pp. 2757-2769
    • Fong, J.C.1    Syed, K.A.2    Klose, K.E.3    Yildiz, F.H.4
  • 13
    • 77955297543 scopus 로고    scopus 로고
    • Growth in a biofilm induces a hyperinfectious phenotype in Vibrio cholerae
    • Tamayo R, Patimalla B, Camilli A. 2010. Growth in a biofilm induces a hyperinfectious phenotype in Vibrio cholerae. Infect. Immun. 78:3560-3569.
    • (2010) Infect. Immun. , vol.78 , pp. 3560-3569
    • Tamayo, R.1    Patimalla, B.2    Camilli, A.3
  • 15
    • 31344435869 scopus 로고    scopus 로고
    • Identification and characterization of RbmA, a novel protein required for the development of rugose colony morphology and biofilm structure in Vibrio cholerae
    • Fong JC, Karplus K, Schoolnik GK, Yildiz FH. 2006. Identification and characterization of RbmA, a novel protein required for the development of rugose colony morphology and biofilm structure in Vibrio cholerae. J. Bacteriol. 188:1049-1059.
    • (2006) J. Bacteriol. , vol.188 , pp. 1049-1059
    • Fong, J.C.1    Karplus, K.2    Schoolnik, G.K.3    Yildiz, F.H.4
  • 16
    • 33947122068 scopus 로고    scopus 로고
    • The rbmBCDEF gene cluster modulates development of rugose colony morphology and biofilm formation in Vibrio cholerae
    • Fong JC, Yildiz FH. 2007. The rbmBCDEF gene cluster modulates development of rugose colony morphology and biofilm formation in Vibrio cholerae. J. Bacteriol. 189:2319-2330.
    • (2007) J. Bacteriol. , vol.189 , pp. 2319-2330
    • Fong, J.C.1    Yildiz, F.H.2
  • 17
    • 0033616585 scopus 로고    scopus 로고
    • Vibrio cholerae O1 El Tor: identification of a gene cluster required for the rugose colony type, exopolysaccharide production, chlorine resistance, and biofilm formation
    • Yildiz FH, Schoolnik GK. 1999. Vibrio cholerae O1 El Tor: identification of a gene cluster required for the rugose colony type, exopolysaccharide production, chlorine resistance, and biofilm formation. Proc. Natl. Acad. Sci. U. S. A. 96:4028-4033.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4028-4033
    • Yildiz, F.H.1    Schoolnik, G.K.2
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 21 -towards automated and web-supported small-angle scattering data analysis.
    • Petoukhov VK, Konarev PV, Kikhney AG, Svergun DI. 2007. ATSAS 2.1 -towards automated and web-supported small-angle scattering data analysis. J. Appl. Cryst. 40:s223-s228.
    • (2007) J. Appl. Cryst. , vol.40
    • Petoukhov, V.K.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 23
    • 79952298783 scopus 로고    scopus 로고
    • Structural basis for the nucleotidedependent dimerization of the large G protein atlastin-1/SPG3A
    • Byrnes LJ, Sondermann H. 2011. Structural basis for the nucleotidedependent dimerization of the large G protein atlastin-1/SPG3A. Proc. Natl. Acad. Sci. U. S. A. 108:2216-2221.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2216-2221
    • Byrnes, L.J.1    Sondermann, H.2
  • 24
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH. 2001. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80:2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 25
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determined in small-angle scattering J
    • Volkov VV, Svergun DI. 2003. Uniqueness of ab initio shape determined in small-angle scattering J. Appl. Cryst. 36:860-864.
    • (2003) Appl. Cryst. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 26
    • 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
  • 28
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased byMADanalysis of the selenomethionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP. 1992. Structure of a fibronectin type III domain from tenascin phased byMADanalysis of the selenomethionyl protein. Science 258:987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 29
    • 79952201735 scopus 로고    scopus 로고
    • Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation
    • De N, Navarro MV, Wang Q, Krasteva PV, Sondermann H. 2010. Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation. Methods Enzymol. 471:161-184.
    • (2010) Methods Enzymol. , vol.471 , pp. 161-184
    • De, N.1    Navarro, M.V.2    Wang, Q.3    Krasteva, P.V.4    Sondermann, H.5
  • 30
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenstrom P. 2010. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38:W545-W549.
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 32
    • 84861990930 scopus 로고    scopus 로고
    • Structural elucidation of dextran degradation mechanism by Streptococcus mutans dextranase belonging to glycoside hydrolase family 66
    • Suzuki N, Kim YM, Fujimoto Z, Momma M, Okuyama M, Mori H, Funane K, Kimura A. 2012. Structural elucidation of dextran degradation mechanism by Streptococcus mutans dextranase belonging to glycoside hydrolase family 66. J. Biol. Chem. 287:19916-19926.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19916-19926
    • Suzuki, N.1    Kim, Y.M.2    Fujimoto, Z.3    Momma, M.4    Okuyama, M.5    Mori, H.6    Funane, K.7    Kimura, A.8
  • 34
    • 1242352009 scopus 로고    scopus 로고
    • The structure of a mycobacterial outer-membrane channel
    • Faller M, Niederweis M, Schulz GE. 2004. The structure of a mycobacterial outer-membrane channel. Science 303:1189-1192.
    • (2004) Science , vol.303 , pp. 1189-1192
    • Faller, M.1    Niederweis, M.2    Schulz, G.E.3
  • 36
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam CD, Hammel M, Hura GL, Tainer JA. 2007. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40:191-285.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 37
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using smallangle scattering in solution
    • Svergun DI, Koch MH. 2002. Advances in structure analysis using smallangle scattering in solution. Curr. Opin. Struct. Biol. 12:654-660.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 654-660
    • Svergun, D.I.1    Koch, M.H.2
  • 38
    • 80052313373 scopus 로고    scopus 로고
    • A communal bacterial adhesin anchors biofilm and bystander cells to surfaces
    • doi:10.1371/journal.ppat.1002210
    • Absalon C, Van Dellen K, Watnick PI. 2011. A communal bacterial adhesin anchors biofilm and bystander cells to surfaces. PLoS Pathog. 7:e1002210. doi:10.1371/journal.ppat.1002210.
    • (2011) PLoS Pathog. , vol.7
    • Absalon, C.1    Van Dellen, K.2    Watnick, P.I.3
  • 39
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • Geiger B, Bershadsky A, Pankov R, Yamada KM. 2001. Transmembrane crosstalk between the extracellular matrix and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2:793-805.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 40
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal protein domain by bacteria
    • Bork P, Doolittle RF. 1992. Proposed acquisition of an animal protein domain by bacteria. Proc. Natl. Acad. Sci. U. S. A. 89:8990-8994.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 42
    • 1642452668 scopus 로고    scopus 로고
    • FnIII domains: predicting mechanical stability
    • Rounsevell RW, Clarke J. 2004. FnIII domains: predicting mechanical stability. Structure 12:4-5.
    • (2004) Structure , vol.12 , pp. 4-5
    • Rounsevell, R.W.1    Clarke, J.2
  • 44
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson HP. 1994. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl. Acad. Sci. U. S. A. 91:10114-10118.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 46
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 47
    • 19244385785 scopus 로고    scopus 로고
    • Folding-unfolding of FN-III domains in tenascin: an elastically coupled two-state system
    • Marin JL, Muniz J, Huerta M, Trujillo X. 2003. Folding-unfolding of FN-III domains in tenascin: an elastically coupled two-state system. J. Biomech. 36:1733-1737.
    • (2003) J. Biomech. , vol.36 , pp. 1733-1737
    • Marin, J.L.1    Muniz, J.2    Huerta, M.3    Trujillo, X.4
  • 48
    • 78650961741 scopus 로고    scopus 로고
    • Factor XIII: novel structural and functional aspects
    • Komaromi I, Bagoly Z, Muszbek L. 2011. Factor XIII: novel structural and functional aspects. J. Thromb. Haemost. 9:9-20. Giglio et al. 3286
    • (2011) J. Thromb. Haemost. , vol.9 , pp. 9-20
    • Komaromi, I.1    Bagoly, Z.2    Muszbek, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.