메뉴 건너뛰기




Volumn 72, Issue 6, 2006, Pages 4044-4053

A mutation in Flavobacterium psychrophilum tlpB inhibits gliding motility and induces biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

BIOFILMS; CYTOLOGY; DNA SEQUENCES; ENZYME KINETICS; PROTEINS; TOXICITY;

EID: 33745121537     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00128-06     Document Type: Article
Times cited : (66)

References (54)
  • 1
    • 0032851954 scopus 로고    scopus 로고
    • Impact of rpoS detection on Escherichia coli biofilm
    • Adams, J. L., and R. J. McLean. 1999. Impact of rpoS detection on Escherichia coli biofilm. Appl. Environ. Microbiol. 65:4285-4287.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4285-4287
    • Adams, J.L.1    McLean, R.J.2
  • 2
    • 0030666570 scopus 로고    scopus 로고
    • Cloning and characterization of the Flavobacterium johnsoniae (Cytophaga johnsonae) gliding motility gene, gldA
    • Agarwal, S., D. W. Hunnicutt, and M. J. McBride. 1997. Cloning and characterization of the Flavobacterium johnsoniae (Cytophaga johnsonae) gliding motility gene, gldA. Proc. Natl. Acad. Sci. USA 94:12139-12144.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12139-12144
    • Agarwal, S.1    Hunnicutt, D.W.2    McBride, M.J.3
  • 3
    • 0347760385 scopus 로고    scopus 로고
    • Development of genetic techniques for the psychrotrophic fish pathogen Flavobacterium psychrophilum
    • Álvarez, B., P. Secades, M. J. McBride, and J. A. Guijarro. 2004. Development of genetic techniques for the psychrotrophic fish pathogen Flavobacterium psychrophilum. Appl. Environ. Microbiol. 70:581-587.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 581-587
    • Álvarez, B.1    Secades, P.2    McBride, M.J.3    Guijarro, J.A.4
  • 4
    • 0021711731 scopus 로고
    • Simple, rapid, and quantitative release of periplasmic proteins by chloroform
    • Ames, G. F.-L., C. Prody, and S. Kustu. 1984. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. J. Bacteriol. 160:1181-1183.
    • (1984) J. Bacteriol. , vol.160 , pp. 1181-1183
    • Ames, G.F.-L.1    Prody, C.2    Kustu, S.3
  • 5
    • 0035403493 scopus 로고    scopus 로고
    • Detection of differential gene expression in biofilm-forming versus planktonic population of Staphylococcus aureus using microrepresentational- difference analysis
    • Becker, P., W. Hufnagle, G. Paters, and M. Herrmann. 2001. Detection of differential gene expression in biofilm-forming versus planktonic population of Staphylococcus aureus using microrepresentational-difference analysis. Appl. Environ. Microbiol. 67:2958-2965.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2958-2965
    • Becker, P.1    Hufnagle, W.2    Paters, G.3    Herrmann, M.4
  • 6
    • 0028154647 scopus 로고
    • Electrophorectic detection of proteases from selected strains of Flexibacter psychrophilus and assessment of their variability
    • Bertolini, J. M., H. Wakabayashi, V. G. Watral, M. J. Whipple, and J. S. Rohovec. 1994. Electrophorectic detection of proteases from selected strains of Flexibacter psychrophilus and assessment of their variability. J. Aquat. Anim. Health 6:224-233.
    • (1994) J. Aquat. Anim. Health , vol.6 , pp. 224-233
    • Bertolini, J.M.1    Wakabayashi, H.2    Watral, V.G.3    Whipple, M.J.4    Rohovec, J.S.5
  • 7
    • 6044239438 scopus 로고    scopus 로고
    • MorA defines a new class of regulators affecting flagellar development and biofilm formation in diverse Pseudomonas species
    • Choy, W.-K., L. Zhou, C. K.-C. Syn, L.-H. Zhang, and S. Swamp. 2004. MorA defines a new class of regulators affecting flagellar development and biofilm formation in diverse Pseudomonas species. J. Bacteriol. 186:7221-7228.
    • (2004) J. Bacteriol. , vol.186 , pp. 7221-7228
    • Choy, W.-K.1    Zhou, L.2    Syn, C.K.-C.3    Zhang, L.-H.4    Swamp, S.5
  • 8
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in bacterial periplasm
    • Chung, J., T. Chen, and D. Missiakas. 2000. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in bacterial periplasm. Mol. Microbiol. 35:1099-1109.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 9
    • 0030810779 scopus 로고    scopus 로고
    • Construction and characterization of a Bacteroides thetaiotaomicron recA mutant: Transfer of Bacteroides integrated conjugative elements is recA independent
    • Cooper, A. J., A. P. Kalinowski, N. B. Shoemaker, and A. A. Salyers. 1997. Construction and characterization of a Bacteroides thetaiotaomicron recA mutant: transfer of Bacteroides integrated conjugative elements is recA independent. J. Bacteriol. 179:6221-6227.
    • (1997) J. Bacteriol. , vol.179 , pp. 6221-6227
    • Cooper, A.J.1    Kalinowski, A.P.2    Shoemaker, N.B.3    Salyers, A.A.4
  • 10
    • 2542430403 scopus 로고    scopus 로고
    • Structural basis of redox-couple protein substrate selection by the cytochrome c biosynthesis protein ResA
    • Crow, A., R. M. Acheson, N. E. Le Brun, and A. Oubrie. 2004. Structural basis of redox-couple protein substrate selection by the cytochrome c biosynthesis protein ResA. J. Biol. Chem. 279:23654-23660.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23654-23660
    • Crow, A.1    Acheson, R.M.2    Le Brun, N.E.3    Oubrie, A.4
  • 11
    • 0036283907 scopus 로고    scopus 로고
    • Usefulness of a TaqMan-based polymerase chain reaction assay for the detection of the fish pathogen Flavobacterium psychrophilum
    • Del Cerro, A., M. C. Mendoza, and J. A. Guijarro. 2002. Usefulness of a TaqMan-based polymerase chain reaction assay for the detection of the fish pathogen Flavobacterium psychrophilum. J. Appl. Microbiol. 93:149-156.
    • (2002) J. Appl. Microbiol. , vol.93 , pp. 149-156
    • Del Cerro, A.1    Mendoza, M.C.2    Guijarro, J.A.3
  • 12
    • 10044220865 scopus 로고    scopus 로고
    • Dynamics and control of biofilm of the oligotrophic bacterium Caulobacter crescentus
    • Entcheva-Dimitrov, P., and A. M. Spormann. 2004. Dynamics and control of biofilm of the oligotrophic bacterium Caulobacter crescentus. J. Bacteriol. 186:8254-8266.
    • (2004) J. Bacteriol. , vol.186 , pp. 8254-8266
    • Entcheva-Dimitrov, P.1    Spormann, A.M.2
  • 13
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
    • Fabianek, R. A., H. Hennecke, and L. Thony-Meyer. 2000. Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli. FEMS Microbiol. Rev. 24:303-316.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 14
    • 0034727049 scopus 로고    scopus 로고
    • Standardization of experimental infection with Flavobacterium psychrophilum, the agent of rainbow trout Onchorhynchus mykiss fry syndrome
    • Garcia, C., F. Pozet, and C. Michel. 2000. Standardization of experimental infection with Flavobacterium psychrophilum, the agent of rainbow trout Onchorhynchus mykiss fry syndrome. Dis. Aquat. Org. 42:191-197.
    • (2000) Dis. Aquat. Org. , vol.42 , pp. 191-197
    • Garcia, C.1    Pozet, F.2    Michel, C.3
  • 15
    • 0029920263 scopus 로고    scopus 로고
    • Alteration in Vibrio cholerae motility phenotypes correlate with changes in virulence factor expression
    • Gardel, C. L., and J. J. Mekalanos. 1996. Alteration in Vibrio cholerae motility phenotypes correlate with changes in virulence factor expression. Infect. Immun. 64:2246-2255.
    • (1996) Infect. Immun. , vol.64 , pp. 2246-2255
    • Gardel, C.L.1    Mekalanos, J.J.2
  • 16
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v. 2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy, J. L., M. R. Laird, F. Chen, S. Rey, C. J. Walsh, M. Ester, and F. S. L. Brinkman. 2005. PSORTb v. 2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21:617-623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.L.7
  • 17
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • Ha, U.-H., Y. Wang, and S. Jin. 2003. DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors. Infect. Immun. 71:1590-1595.
    • (2003) Infect. Immun. , vol.71 , pp. 1590-1595
    • Ha, U.-H.1    Wang, Y.2    Jin, S.3
  • 18
    • 0017653811 scopus 로고
    • Bovine thioredoxin system
    • Holmgren, A. 1977. Bovine thioredoxin system. J. Biol. Chem. 252:4600-4606.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 19
    • 0036226255 scopus 로고    scopus 로고
    • Mutations in Flavobacterium johnsoniae gldF and gldG disrupt gliding motility and interfere with membrane localization of GldA
    • Hunnicutt, D. W., M. J. Kempf, and M. J. McBride. 2002. Mutations in Flavobacterium johnsoniae gldF and gldG disrupt gliding motility and interfere with membrane localization of GldA. J. Bacteriol. 184:2370-2378.
    • (2002) J. Bacteriol. , vol.184 , pp. 2370-2378
    • Hunnicutt, D.W.1    Kempf, M.J.2    McBride, M.J.3
  • 20
    • 0033978998 scopus 로고    scopus 로고
    • Cloning and characterization of the Flavobacterium johnsoniae gliding-motility genes gldB and gldC
    • Hunnicutt, D. W., and M. J. McBride. 2000. Cloning and characterization of the Flavobacterium johnsoniae gliding-motility genes gldB and gldC. J. Bacteriol. 182:911-918.
    • (2000) J. Bacteriol. , vol.182 , pp. 911-918
    • Hunnicutt, D.W.1    McBride, M.J.2
  • 21
    • 0034972737 scopus 로고    scopus 로고
    • Cloning and characterization of the Flavobacterium johnsoniae gliding motility genes gldD and gldE
    • Hunnicutt, D. W., and M. J. McBride. 2001. Cloning and characterization of the Flavobacterium johnsoniae gliding motility genes gldD and gldE. J. Bacteriol. 183:4167-4175.
    • (2001) J. Bacteriol. , vol.183 , pp. 4167-4175
    • Hunnicutt, D.W.1    McBride, M.J.2
  • 22
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L. A., R. M. MacCallum, and M. J. Stember. 2000. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Stember, M.J.3
  • 24
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • Luthman, M., and A. Holmgren. 1982. Rat liver thioredoxin and thioredoxin reductase: purification and characterization. Biochemistry 21:6628-6633.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 26
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin, J. L. 1995. Thioredoxin: a fold for all reasons. Structure 3:245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 27
    • 2642529310 scopus 로고    scopus 로고
    • Cytophaga-Flavobacterium gliding motility
    • McBride, M. J. 2004. Cytophaga-Flavobacterium gliding motility. J. Mol. Microbiol. Biotechnol. 7:63-71.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 63-71
    • McBride, M.J.1
  • 28
    • 1842559428 scopus 로고    scopus 로고
    • GldI is a lipoprotein that is required for Flavobacterium johnsoniae gliding motility and cnitin utilization
    • McBride, M. J., and T. F. Braun. 2004. GldI is a lipoprotein that is required for Flavobacterium johnsoniae gliding motility and cnitin utilization. J. Bacteriol. 186:2295-2302.
    • (2004) J. Bacteriol. , vol.186 , pp. 2295-2302
    • McBride, M.J.1    Braun, T.F.2
  • 29
    • 0242407469 scopus 로고    scopus 로고
    • Flavobacterium johnsoniae GldH is a lipoprotein that is required for gliding motility and chitin utilization
    • McBride, M. J., T. F. Braun, and J. L. Brust. 2003. Flavobacterium johnsoniae GldH is a lipoprotein that is required for gliding motility and chitin utilization. J. Bacteriol. 185:6648-6657.
    • (2003) J. Bacteriol. , vol.185 , pp. 6648-6657
    • McBride, M.J.1    Braun, T.F.2    Brust, J.L.3
  • 30
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 31
    • 0027787823 scopus 로고
    • The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas, J., P. E. Rouviere, J. W. Erickson, T. J. Donohue, and C. A. Gross. 1993. The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev. 7:2618-2628.
    • (1993) Genes Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 32
    • 0028221665 scopus 로고
    • Use of the rep technique for allele replacement to construct new Escherichia coli hosts for maintenance of R6Kγ origin plasmids at different copy numbers
    • Metcalf, W. W., W. Jiang, and B. L. Wanner. 1994. Use of the rep technique for allele replacement to construct new Escherichia coli hosts for maintenance of R6Kγ origin plasmids at different copy numbers. Gene 138:1-7.
    • (1994) Gene , vol.138 , pp. 1-7
    • Metcalf, W.W.1    Jiang, W.2    Wanner, B.L.3
  • 33
    • 0032705847 scopus 로고    scopus 로고
    • Production of viable cultures of Flavobacterium psychrophilum approach and control
    • Michel, C., D. Antonio, and R. P. Hedrick. 1999. Production of viable cultures of Flavobacterium psychrophilum approach and control. Res. Microbiol. 150:351-358.
    • (1999) Res. Microbiol. , vol.150 , pp. 351-358
    • Michel, C.1    Antonio, D.2    Hedrick, R.P.3
  • 34
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D., and S. Raina. 1997. Protein folding in the bacterial periplasm. J. Bacteriol. 179:2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 35
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., F. Schwager, and S. Raina. 1995. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:3415-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 36
    • 0141816847 scopus 로고    scopus 로고
    • Involvement of a sialic acid-binding lectin with hemagglutination and hydrophobicity of Flavobacterium psychrophilum
    • Møller, J. D., J. L. Larsen, L. Madsen, and I. Dalsgaard. 2003. Involvement of a sialic acid-binding lectin with hemagglutination and hydrophobicity of Flavobacterium psychrophilum. Appl. Environ. Microbiol. 69:5275-5280.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5275-5280
    • Møller, J.D.1    Larsen, J.L.2    Madsen, L.3    Dalsgaard, I.4
  • 37
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto, H., and J. C. A. Bardwell. 2004. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochem. Biophys. Acta 1694:111-119.
    • (2004) Biochem. Biophys. Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.A.2
  • 39
    • 0042769061 scopus 로고    scopus 로고
    • Adhesion of high and low virulence Flavobacterium psychrophilum strains to isolated gill arches of rainbow trout Oncorhynchus mykiis
    • Nematollahi, A., A. Decostere, F. Pasmas, R. Ducatelle, and F. Haesebrouck. 2003. Adhesion of high and low virulence Flavobacterium psychrophilum strains to isolated gill arches of rainbow trout Oncorhynchus mykiis. Dis. Aquat. Org. 55:101-107.
    • (2003) Dis. Aquat. Org. , vol.55 , pp. 101-107
    • Nematollahi, A.1    Decostere, A.2    Pasmas, F.3    Ducatelle, R.4    Haesebrouck, F.5
  • 40
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol: Disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
    • Peek, J. A., and R. K. Taylor. 1992. Characterization of a periplasmic thiol: disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl. Acad. Sci. USA 89: 6210-6214.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 41
    • 4544258776 scopus 로고    scopus 로고
    • The unusual transmembrane electron transporter DsbD and its homologues: A bacterial family of disulfide reductases
    • Porat, A., S.-H. Cho, and J. Beckwith. 2004. The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res. Microbiol. 155:617-622.
    • (2004) Res. Microbiol. , vol.155 , pp. 617-622
    • Porat, A.1    Cho, S.-H.2    Beckwith, J.3
  • 42
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: Roles of flagella, motility, chemotaxis and type I pili
    • Pratt, L. A., and R. Kolter. 1998. Genetic analysis of Escherichia coli biofilm formation: roles of flagella, motility, chemotaxis and type I pili. Mol. Microbiol. 30:285-293.
    • (1998) Mol. Microbiol. , vol.30 , pp. 285-293
    • Pratt, L.A.1    Kolter, R.2
  • 44
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli
    • Raina, S., D. Missiakas, and C. Georgopoulos. 1995. The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J. 14:1043-1055.
    • (1995) EMBO J. , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 45
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed, L. J., and H. Muench. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 46
    • 0035375081 scopus 로고    scopus 로고
    • Purification and characterization of a psychrophilic calcium-induced, growth-phase-dependent metalloprotease from the fish pathogen Flavobacterium psychrophilum
    • Secades, P., B. Álvarez, and J. A. Guijarro. 2001. Purification and characterization of a psychrophilic calcium-induced, growth-phase-dependent metalloprotease from the fish pathogen Flavobacterium psychrophilum. Appl. Environ. Microbiol. 67:2436-2444.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2436-2444
    • Secades, P.1    Álvarez, B.2    Guijarro, J.A.3
  • 47
    • 0642347021 scopus 로고    scopus 로고
    • Purification and properties of a new psychrophilic metalloprotease (Fpp2) in the fish pathogen Flavobacterium psychrophilum
    • Secades P., B. Álvarez, and J. A. Guijarro. 2003. Purification and properties of a new psychrophilic metalloprotease (Fpp2) in the fish pathogen Flavobacterium psychrophilum. FEMS Microbiol. Lett. 226:273-279.
    • (2003) FEMS Microbiol. Lett. , vol.226 , pp. 273-279
    • Secades, P.1    Álvarez, B.2    Guijarro, J.A.3
  • 48
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 49
    • 0026588633 scopus 로고
    • Heterologous gene expression in Bacteroides fragilis
    • Smith, C. J., M. B. Rogers, and M. L. McKee. 1992. Heterologous gene expression in Bacteroides fragilis. Plasmid 27:141-154.
    • (1992) Plasmid , vol.27 , pp. 141-154
    • Smith, C.J.1    Rogers, M.B.2    McKee, M.L.3
  • 50
    • 19744372620 scopus 로고    scopus 로고
    • Combining suppression subtractive hybridization and microarrays to map the intraspecies phylogeny of Flavobacterium psychrophilum
    • Soule, M., K. Cain, S. LaFrentz, and D. R. Call. 2005. Combining suppression subtractive hybridization and microarrays to map the intraspecies phylogeny of Flavobacterium psychrophilum. Infect. Immun. 73:3799-3802.
    • (2005) Infect. Immun. , vol.73 , pp. 3799-3802
    • Soule, M.1    Cain, K.2    Lafrentz, S.3    Call, D.R.4
  • 51
    • 0036117802 scopus 로고    scopus 로고
    • DsbA and DsbC are required for secretion of pertussis toxin by Bordetalle pertussis
    • Stenson, T. H., and A. A. Weiss. 2002. DsbA and DsbC are required for secretion of pertussis toxin by Bordetalle pertussis. Infect. Immun. 70:2297-2303.
    • (2002) Infect. Immun. , vol.70 , pp. 2297-2303
    • Stenson, T.H.1    Weiss, A.A.2
  • 53
    • 0036955805 scopus 로고    scopus 로고
    • Multiple Streptococcus mutants genes are involved in biofilm formation
    • Yoshida, A., and H. K. Kuramitsu. 2002. Multiple Streptococcus mutants genes are involved in biofilm formation. Appl. Environ. Microbiol. 68:6283-6291.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6283-6291
    • Yoshida, A.1    Kuramitsu, H.K.2
  • 54
    • 0032786363 scopus 로고    scopus 로고
    • DsbA: A protein-folding catalyst contributing to bacterial virulence
    • Yu, J., and J. S. Kroll. 1999. DsbA: a protein-folding catalyst contributing to bacterial virulence. Microbes Infect. 1:1221-1228.
    • (1999) Microbes Infect. , vol.1 , pp. 1221-1228
    • Yu, J.1    Kroll, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.