메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Growth of acinetobacter baumannii in pellicle enhanced the expression of potential virulence factors

Author keywords

[No Author keywords available]

Indexed keywords

ACINETOBACTIN PROTEIN; BACTERIAL PROTEIN; CARO PROTEIN; ENTEROCHELIN; FERRIC ION; MEMBRANE PROTEIN; OPRD PROTEIN; PORIN; RECEPTOR PROTEIN; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 80055090641     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026030     Document Type: Article
Times cited : (67)

References (84)
  • 1
    • 36248932659 scopus 로고    scopus 로고
    • An increasing threat in hospitals: multidrug-resistant Acinetobacter baumannii
    • Dijkshoom L, Nemec A, Seifert H, (2007) An increasing threat in hospitals: multidrug-resistant Acinetobacter baumannii. Nature Rev Microbiol 5: 939-951.
    • (2007) Nature Rev Microbiol , vol.5 , pp. 939-951
    • Dijkshoom, L.1    Nemec, A.2    Seifert, H.3
  • 2
    • 47949089607 scopus 로고    scopus 로고
    • Acinetobacter baumannii: emergence of a successful pathogen
    • Peleg AY, Seifert H, Paterson DL, (2008) Acinetobacter baumannii: emergence of a successful pathogen. Clin Microbiol Rev 21: 538-582.
    • (2008) Clin Microbiol Rev , vol.21 , pp. 538-582
    • Peleg, A.Y.1    Seifert, H.2    Paterson, D.L.3
  • 3
    • 64149096217 scopus 로고    scopus 로고
    • The genus Acinetobacter
    • Towner KJ, (2006) The genus Acinetobacter. Prokaryotes 6: 746-758.
    • (2006) Prokaryotes , vol.6 , pp. 746-758
    • Towner, K.J.1
  • 4
    • 0034443286 scopus 로고    scopus 로고
    • Microbial biofilms: from ecology to molecular genetics
    • Davey ME, O'Toole GA, (2000) Microbial biofilms: from ecology to molecular genetics. Microbiol Mol Biol Rev 64: 847-867.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 847-867
    • Davey, M.E.1    O'Toole, G.A.2
  • 5
    • 0346252347 scopus 로고    scopus 로고
    • Attachment to and biofilm formation on abiotic surfaces by Acinetobacter baumannii: involvement of a novel chaperone-usher pili assembly system
    • Tomaras AP, Dorsey CW, Edelmann RE, Actis LA, (2003) Attachment to and biofilm formation on abiotic surfaces by Acinetobacter baumannii: involvement of a novel chaperone-usher pili assembly system. Microbiology 149: 3473-3484.
    • (2003) Microbiology , vol.149 , pp. 3473-3484
    • Tomaras, A.P.1    Dorsey, C.W.2    Edelmann, R.E.3    Actis, L.A.4
  • 7
    • 66849142315 scopus 로고    scopus 로고
    • Evolving concepts in biofilm infections
    • Hall-Stoodley L, Stoodley P, (2009) Evolving concepts in biofilm infections. Cell Microbiol 11: 1034-1043.
    • (2009) Cell Microbiol , vol.11 , pp. 1034-1043
    • Hall-Stoodley, L.1    Stoodley, P.2
  • 9
    • 29144475453 scopus 로고    scopus 로고
    • Immobilization induces alterations in the outer membrane protein pattern of Yersinia ruckeri
    • Coquet L, Cosette P, De E, Galas L, Vaudry H, et al. (2005) Immobilization induces alterations in the outer membrane protein pattern of Yersinia ruckeri. J Proteome Res 4: 1988-1998.
    • (2005) J Proteome Res , vol.4 , pp. 1988-1998
    • Coquet, L.1    Cosette, P.2    De, E.3    Galas, L.4    Vaudry, H.5
  • 10
    • 0036157549 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm
    • Sauer K, Camper AK, Ehrlich GD, Costerton JW, Davies DG, (2002) Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm. J Bacteriol 184: 1140-1154.
    • (2002) J Bacteriol , vol.184 , pp. 1140-1154
    • Sauer, K.1    Camper, A.K.2    Ehrlich, G.D.3    Costerton, J.W.4    Davies, D.G.5
  • 11
    • 2342622660 scopus 로고    scopus 로고
    • Comparative proteomic analysis of planktonic and immobilized Pseudomonas aeruginosa cells: a multivariate statistical approach
    • Vilain S, Cosette P, Hubert M, Lange C, Junter GA, et al. (2004) Comparative proteomic analysis of planktonic and immobilized Pseudomonas aeruginosa cells: a multivariate statistical approach. Anal Biochem 329: 120-130.
    • (2004) Anal Biochem , vol.329 , pp. 120-130
    • Vilain, S.1    Cosette, P.2    Hubert, M.3    Lange, C.4    Junter, G.A.5
  • 12
    • 1242297814 scopus 로고    scopus 로고
    • Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms
    • Friedman L, Kolter R, (2004) Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms. Mol Microbiol 51: 675-690.
    • (2004) Mol Microbiol , vol.51 , pp. 675-690
    • Friedman, L.1    Kolter, R.2
  • 13
    • 66849089254 scopus 로고    scopus 로고
    • Characterization of a novel air-liquid interface biofilm of Pseudomonas fluorescens SBW25
    • Koza A, Hallett PD, Moon CD, Spiers AJ, (2009) Characterization of a novel air-liquid interface biofilm of Pseudomonas fluorescens SBW25. Microbiology 155: 1397-1406.
    • (2009) Microbiology , vol.155 , pp. 1397-1406
    • Koza, A.1    Hallett, P.D.2    Moon, C.D.3    Spiers, A.J.4
  • 14
    • 24944465764 scopus 로고    scopus 로고
    • The Pseudomonas fluorescens SBW25 wrinkly spreader biofilm requires attachment factor, cellulose fibre and LPS interactions to maintain strength and integrity
    • Spiers AJ, Rainey PB, (2005) The Pseudomonas fluorescens SBW25 wrinkly spreader biofilm requires attachment factor, cellulose fibre and LPS interactions to maintain strength and integrity. Microbiology 151: 2829-2839.
    • (2005) Microbiology , vol.151 , pp. 2829-2839
    • Spiers, A.J.1    Rainey, P.B.2
  • 15
    • 78651096892 scopus 로고    scopus 로고
    • Biofilm formation at the solid-liquid and air-liquid interfaces by Acinetobacter species
    • Marti S, Rodriguez-Bano J, Catel-Ferreira M, Jouenne T, Vila J, et al. (2011) Biofilm formation at the solid-liquid and air-liquid interfaces by Acinetobacter species. BMC Res Notes 4: 5-8.
    • (2011) BMC Res Notes , vol.4 , pp. 5-8
    • Marti, S.1    Rodriguez-Bano, J.2    Catel-Ferreira, M.3    Jouenne, T.4    Vila, J.5
  • 17
    • 0036125317 scopus 로고    scopus 로고
    • Activity of clinafloxacin, compared with six other quinolones, against Acinetobacter baumannii clinical isolates
    • Vila J, Ribera A, Marco F, Ruiz J, Mensa J, et al. (2002) Activity of clinafloxacin, compared with six other quinolones, against Acinetobacter baumannii clinical isolates. J Antimicrob Chemother 49: 471-477.
    • (2002) J Antimicrob Chemother , vol.49 , pp. 471-477
    • Vila, J.1    Ribera, A.2    Marco, F.3    Ruiz, J.4    Mensa, J.5
  • 18
    • 33845467685 scopus 로고    scopus 로고
    • Proteomic analysis of a fraction enriched in cell envelope proteins of Acinetobacter baumannii
    • Marti S, Sanchez-Cespedes J, Oliveira E, Bellido D, Giralt E, et al. (2006) Proteomic analysis of a fraction enriched in cell envelope proteins of Acinetobacter baumannii. Proteomics 6: 82-87.
    • (2006) Proteomics , vol.6 , pp. 82-87
    • Marti, S.1    Sanchez-Cespedes, J.2    Oliveira, E.3    Bellido, D.4    Giralt, E.5
  • 19
    • 0002476741 scopus 로고
    • Silver-staining of proteins in polyacrylamide gels: a general overview
    • Rabilloud T, Vuillard L, Gilly C, Lawrence JJ, (1994) Silver-staining of proteins in polyacrylamide gels: a general overview. Cell Mol Biol 40: 57-75.
    • (1994) Cell Mol Biol , vol.40 , pp. 57-75
    • Rabilloud, T.1    Vuillard, L.2    Gilly, C.3    Lawrence, J.J.4
  • 20
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis
    • O'Toole GA, Kolter R, (1998) Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis. Mol Microbiol 28: 449-461.
    • (1998) Mol Microbiol , vol.28 , pp. 449-461
    • O'Toole, G.A.1    Kolter, R.2
  • 21
    • 33144490023 scopus 로고    scopus 로고
    • Comparative genomics of multidrug resistance in Acinetobacter baumannii
    • Fournier PE, Vallenet D, Barbe V, Audic S, Ogata H, et al. (2006) Comparative genomics of multidrug resistance in Acinetobacter baumannii. PLoS Genet 2: e7.
    • (2006) PLoS Genet , vol.2
    • Fournier, P.E.1    Vallenet, D.2    Barbe, V.3    Audic, S.4    Ogata, H.5
  • 22
    • 33144475257 scopus 로고    scopus 로고
    • The thin pili of Acinetobacter sp. strain BD413 mediate adhesion to biotic and abiotic surfaces
    • Gohl O, Friedrich A, Hoppert M, Averhoff B, (2006) The thin pili of Acinetobacter sp. strain BD413 mediate adhesion to biotic and abiotic surfaces. Appl Environ Microbiol 72: 1394-1401.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1394-1401
    • Gohl, O.1    Friedrich, A.2    Hoppert, M.3    Averhoff, B.4
  • 23
    • 35348928659 scopus 로고    scopus 로고
    • Morphological analysis of young and old pellicles of Salmonella Typhimurium
    • Scher K, Kesselman E, Shimoni E, Yaron S, (2007) Morphological analysis of young and old pellicles of Salmonella Typhimurium. Biofouling 23: 385-394.
    • (2007) Biofouling , vol.23 , pp. 385-394
    • Scher, K.1    Kesselman, E.2    Shimoni, E.3    Yaron, S.4
  • 24
    • 0029860794 scopus 로고    scopus 로고
    • Influence of relative humidity and suspending menstrua on survival of Acinetobacter spp on dry surfaces
    • Jawad A, Heritage J, Snelling AM, Gascoyne-Binzi DM, Hawkey PM, (1996) Influence of relative humidity and suspending menstrua on survival of Acinetobacter spp on dry surfaces. J Clin Microbiol 34: 2881-2887.
    • (1996) J Clin Microbiol , vol.34 , pp. 2881-2887
    • Jawad, A.1    Heritage, J.2    Snelling, A.M.3    Gascoyne-Binzi, D.M.4    Hawkey, P.M.5
  • 25
    • 0031808598 scopus 로고    scopus 로고
    • Survival of Acinetobacter baumannii on dry surfaces: comparison of outbreak and sporadic isolates
    • Jawad A, Seifert H, Snelling AM, Heritage J, Hawkey PM, (1998) Survival of Acinetobacter baumannii on dry surfaces: comparison of outbreak and sporadic isolates. J Clin Microbiol 36: 1938-1941.
    • (1998) J Clin Microbiol , vol.36 , pp. 1938-1941
    • Jawad, A.1    Seifert, H.2    Snelling, A.M.3    Heritage, J.4    Hawkey, P.M.5
  • 26
    • 0033306554 scopus 로고    scopus 로고
    • Multiple environmental factors regulate the expression of the carbohydrate-selective OprB porin of Pseudomonas aeruginosa
    • Adewoye LO, Worobec EA, (1999) Multiple environmental factors regulate the expression of the carbohydrate-selective OprB porin of Pseudomonas aeruginosa. Can J Microbiol 45: 1033-1042.
    • (1999) Can J Microbiol , vol.45 , pp. 1033-1042
    • Adewoye, L.O.1    Worobec, E.A.2
  • 27
    • 0028847646 scopus 로고
    • Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus
    • Leisman GB, Waukau J, Forst SA, (1995) Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus. Appl Environ Microbiol 61: 200-204.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 200-204
    • Leisman, G.B.1    Waukau, J.2    Forst, S.A.3
  • 28
    • 0030937090 scopus 로고    scopus 로고
    • A phosphate-starvation-inducible outer-membrane protein of Pseudomonas fluorescens Ag1 as an immunological phosphate-starvation marker
    • Leopold K, Jacobsen S, Nybroe O, (1997) A phosphate-starvation-inducible outer-membrane protein of Pseudomonas fluorescens Ag1 as an immunological phosphate-starvation marker. Microbiology 143: 1019-1027.
    • (1997) Microbiology , vol.143 , pp. 1019-1027
    • Leopold, K.1    Jacobsen, S.2    Nybroe, O.3
  • 29
    • 0036062240 scopus 로고    scopus 로고
    • pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli
    • Stancik LM, Stancik DM, Schmidt B, Barnhart DM, Yoncheva YN, et al. (2002) pH-dependent expression of periplasmic proteins and amino acid catabolism in Escherichia coli. J Bacteriol 184: 4246-4258.
    • (2002) J Bacteriol , vol.184 , pp. 4246-4258
    • Stancik, L.M.1    Stancik, D.M.2    Schmidt, B.3    Barnhart, D.M.4    Yoncheva, Y.N.5
  • 30
    • 34447556772 scopus 로고    scopus 로고
    • Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii
    • Vila J, Marti S, Sanchez-Cespedes J, (2007) Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii. J Antimicrob Chemother 59: 1210-1215.
    • (2007) J Antimicrob Chemother , vol.59 , pp. 1210-1215
    • Vila, J.1    Marti, S.2    Sanchez-Cespedes, J.3
  • 31
    • 17444377003 scopus 로고    scopus 로고
    • Characterization and quantitation of membrane proteomes using multidimensional MS-based proteomic technologies
    • Blonder J, Conrads TP, Veenstra TD, (2004) Characterization and quantitation of membrane proteomes using multidimensional MS-based proteomic technologies. Expert Rev Proteomics 1: 153-163.
    • (2004) Expert Rev Proteomics , vol.1 , pp. 153-163
    • Blonder, J.1    Conrads, T.P.2    Veenstra, T.D.3
  • 32
    • 33845450679 scopus 로고    scopus 로고
    • Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain
    • Siroy A, Cosette P, Seyer D, Lemaitre-Guillier C, Vallenet D, et al. (2006) Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain. J Proteome Res 5: 3385-3398.
    • (2006) J Proteome Res , vol.5 , pp. 3385-3398
    • Siroy, A.1    Cosette, P.2    Seyer, D.3    Lemaitre-Guillier, C.4    Vallenet, D.5
  • 33
    • 20444463103 scopus 로고    scopus 로고
    • Proteomic comparison of outer membrane protein patterns of sessile and planktonic Pseudomonas aeruginosa cells
    • Seyer D, Cosette P, Siroy A, De E, Lenz C, et al. (2005) Proteomic comparison of outer membrane protein patterns of sessile and planktonic Pseudomonas aeruginosa cells. Biofilms 2: 27-36.
    • (2005) Biofilms , vol.2 , pp. 27-36
    • Seyer, D.1    Cosette, P.2    Siroy, A.3    De, E.4    Lenz, C.5
  • 34
    • 10744232444 scopus 로고    scopus 로고
    • Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression
    • Beloin C, Valle J, Latour-Lambert P, Faure P, Kzreminski M, et al. (2004) Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression. Mol Microbiol 51: 659-674.
    • (2004) Mol Microbiol , vol.51 , pp. 659-674
    • Beloin, C.1    Valle, J.2    Latour-Lambert, P.3    Faure, P.4    Kzreminski, M.5
  • 35
    • 78349246336 scopus 로고    scopus 로고
    • Physiology of Pseudomonas aeruginosa in biofilms as revealed by transcriptome analysis
    • Folsom JP, Richards L, Pitts B, Roe F, Ehrlich GD, et al. (2010) Physiology of Pseudomonas aeruginosa in biofilms as revealed by transcriptome analysis. BMC Microbiol 10: 294.
    • (2010) BMC Microbiol , vol.10 , pp. 294
    • Folsom, J.P.1    Richards, L.2    Pitts, B.3    Roe, F.4    Ehrlich, G.D.5
  • 37
    • 58149383896 scopus 로고    scopus 로고
    • Impact of rpoS deletion on the proteome of Escherichia coli grown planktonically and as biofilm
    • Collet A, Cosette P, Beloin C, Ghigo JM, Rihouey C, et al. (2008) Impact of rpoS deletion on the proteome of Escherichia coli grown planktonically and as biofilm. J Proteome Res 7: 4659-4669.
    • (2008) J Proteome Res , vol.7 , pp. 4659-4669
    • Collet, A.1    Cosette, P.2    Beloin, C.3    Ghigo, J.M.4    Rihouey, C.5
  • 39
    • 74549214393 scopus 로고    scopus 로고
    • Growth in glucose-based medium and exposure to subinhibitory concentrations of imipenem induce biofilm formation in a multidrug-resistant clinical isolate of Acinetobacter baumannii
    • Nucleo E, Steffanoni L, Fugazza G, Migliavacca R, Giacobone E, et al. (2009) Growth in glucose-based medium and exposure to subinhibitory concentrations of imipenem induce biofilm formation in a multidrug-resistant clinical isolate of Acinetobacter baumannii. BMC Microbiol 9: 270.
    • (2009) BMC Microbiol , vol.9 , pp. 270
    • Nucleo, E.1    Steffanoni, L.2    Fugazza, G.3    Migliavacca, R.4    Giacobone, E.5
  • 40
    • 70350518304 scopus 로고    scopus 로고
    • Effects of iron depletion on antimicrobial activities against planktonic and biofilm Pseudomonas aeruginosa
    • Cai Y, Yu XH, Wang R, An MM, Liang BB, (2009) Effects of iron depletion on antimicrobial activities against planktonic and biofilm Pseudomonas aeruginosa. J Pharm Pharmacol 61: 1257-1262.
    • (2009) J Pharm Pharmacol , vol.61 , pp. 1257-1262
    • Cai, Y.1    Yu, X.H.2    Wang, R.3    An, M.M.4    Liang, B.B.5
  • 41
    • 22544441350 scopus 로고    scopus 로고
    • Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa
    • Musk DJ, Banko DA, Hergenrother PJ, (2005) Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa. Chem Biol 12: 789-796.
    • (2005) Chem Biol , vol.12 , pp. 789-796
    • Musk, D.J.1    Banko, D.A.2    Hergenrother, P.J.3
  • 42
    • 34249049190 scopus 로고    scopus 로고
    • Effects of iron on DNA release and biofilm development by Pseudomonas aeruginosa
    • Yang L, Barken KB, Skindersoe ME, Christensen AB, Givskov M, et al. (2007) Effects of iron on DNA release and biofilm development by Pseudomonas aeruginosa. Microbiology 153: 1318-1328.
    • (2007) Microbiology , vol.153 , pp. 1318-1328
    • Yang, L.1    Barken, K.B.2    Skindersoe, M.E.3    Christensen, A.B.4    Givskov, M.5
  • 43
    • 75949088945 scopus 로고    scopus 로고
    • Proteomic analysis of Acinetobacter baumannii in biofilm and planktonic growth mode
    • Shin JH, Lee HW, Kim SM, Kim J, (2009) Proteomic analysis of Acinetobacter baumannii in biofilm and planktonic growth mode. Journal of Microbiology 47: 728-735.
    • (2009) Journal of Microbiology , vol.47 , pp. 728-735
    • Shin, J.H.1    Lee, H.W.2    Kim, S.M.3    Kim, J.4
  • 45
    • 46349095831 scopus 로고    scopus 로고
    • Comparative analysis of Acinetobacters: Three genomes for three lifestyles
    • Vallenet D, Nordmann P, Barbe V, Poirel L, Mangenot S, (2008) Comparative analysis of Acinetobacters: Three genomes for three lifestyles. PLoS ONE 3: e1805.
    • (2008) PLoS ONE , vol.3
    • Vallenet, D.1    Nordmann, P.2    Barbe, V.3    Poirel, L.4    Mangenot, S.5
  • 46
    • 0035094206 scopus 로고    scopus 로고
    • Adhesion of type 1-fimbriated Escherichia coli to abiotic surfaces leads to altered composition of outer membrane proteins
    • Otto K, Norbeck J, Larsson T, Karlsson KA, Hermansson M, (2001) Adhesion of type 1-fimbriated Escherichia coli to abiotic surfaces leads to altered composition of outer membrane proteins. J Bacteriol 183: 2445-2453.
    • (2001) J Bacteriol , vol.183 , pp. 2445-2453
    • Otto, K.1    Norbeck, J.2    Larsson, T.3    Karlsson, K.A.4    Hermansson, M.5
  • 47
    • 78649892086 scopus 로고    scopus 로고
    • Deciphering the iron response in Acinetobacter baumannii: A proteomics approach
    • Nwugo CC, Gaddy JA, Zimbler DL, Actis LA, (2011) Deciphering the iron response in Acinetobacter baumannii: A proteomics approach. J Proteomics 74: 44-58.
    • (2011) J Proteomics , vol.74 , pp. 44-58
    • Nwugo, C.C.1    Gaddy, J.A.2    Zimbler, D.L.3    Actis, L.A.4
  • 48
    • 30944444979 scopus 로고    scopus 로고
    • Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility
    • Barrios AF, Zuo R, Ren D, Wood TK, (2006) Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility. Biotechnol Bioeng 93: 188-200.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 188-200
    • Barrios, A.F.1    Zuo, R.2    Ren, D.3    Wood, T.K.4
  • 49
    • 67651235793 scopus 로고    scopus 로고
    • The Acinetobacter baumannii 19606 OmpA protein plays a role in biofilm formation on abiotic surfaces and in the interaction of this pathogen with eukaryotic cells
    • Gaddy JA, Tomaras AP, Actis LA, (2009) The Acinetobacter baumannii 19606 OmpA protein plays a role in biofilm formation on abiotic surfaces and in the interaction of this pathogen with eukaryotic cells. Infect Immun 77: 3150-3160.
    • (2009) Infect Immun , vol.77 , pp. 3150-3160
    • Gaddy, J.A.1    Tomaras, A.P.2    Actis, L.A.3
  • 50
    • 70349684496 scopus 로고    scopus 로고
    • OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system
    • Ma Q, Wood TK, (2009) OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system. Environmental Microbiology 11: 2735-2746.
    • (2009) Environmental Microbiology , vol.11 , pp. 2735-2746
    • Ma, Q.1    Wood, T.K.2
  • 51
    • 0037133315 scopus 로고    scopus 로고
    • Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway
    • Otto K, Silhavy TJ, (2002) Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway. Proc Natl Acad Sci U S A 99: 2287-2292.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2287-2292
    • Otto, K.1    Silhavy, T.J.2
  • 52
    • 14644436333 scopus 로고    scopus 로고
    • Simultaneous force and fluorescence measurements of a protein that forms a bond between a living bacterium and a solid surface
    • Lower BH, Yongsunthon R, Vellano FP III, Lower SK, (2005) Simultaneous force and fluorescence measurements of a protein that forms a bond between a living bacterium and a solid surface. J Bacteriol 187: 2127-2137.
    • (2005) J Bacteriol , vol.187 , pp. 2127-2137
    • Lower, B.H.1    Yongsunthon, R.2    Vellano III, F.P.3    Lower, S.K.4
  • 53
    • 33947145569 scopus 로고    scopus 로고
    • New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis
    • Smith MG, Gianoulis TA, Pukatzki S, Mekalanos JJ, Ornston LN, et al. (2007) New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis. Genes Dev 21: 601-614.
    • (2007) Genes Dev , vol.21 , pp. 601-614
    • Smith, M.G.1    Gianoulis, T.A.2    Pukatzki, S.3    Mekalanos, J.J.4    Ornston, L.N.5
  • 54
  • 55
    • 16244406203 scopus 로고    scopus 로고
    • Acquisition of resistance to carbapenems in multidrug-resistant clinical strains of Acinetobacter baumannii: natural insertional inactivation of a gene encoding a member of a novel family of beta-barrel outer membrane proteins
    • Mussi MA, Limansky AS, Viale AM, (2005) Acquisition of resistance to carbapenems in multidrug-resistant clinical strains of Acinetobacter baumannii: natural insertional inactivation of a gene encoding a member of a novel family of beta-barrel outer membrane proteins. Antimicrob Agents Chemother 49: 1432-1440.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1432-1440
    • Mussi, M.A.1    Limansky, A.S.2    Viale, A.M.3
  • 56
    • 36549000278 scopus 로고    scopus 로고
    • CarO, an Acinetobacter baumannii outer membrane protein involved in carbapenem resistance, is essential for L-ornithine uptake
    • Mussi MA, Relling VM, Limansky AS, Viale AM, (2007) CarO, an Acinetobacter baumannii outer membrane protein involved in carbapenem resistance, is essential for L-ornithine uptake. FEBS Lett 581: 5573-5578.
    • (2007) FEBS Lett , vol.581 , pp. 5573-5578
    • Mussi, M.A.1    Relling, V.M.2    Limansky, A.S.3    Viale, A.M.4
  • 57
    • 31844433824 scopus 로고    scopus 로고
    • Biochemical and physical properties of siderophores
    • In: Crosa JH, Mey AR, Payne SM, editors, ASM press
    • Raymond K, Dertz E, (2004) Biochemical and physical properties of siderophores. In: Crosa JH, Mey AR, Payne SM, editors. Iron transport in bacteria ASM press pp. 3-17.
    • (2004) Iron Transport in Bacteria , pp. 3-17
    • Raymond, K.1    Dertz, E.2
  • 58
    • 33846600871 scopus 로고    scopus 로고
    • Characterization of OpdH, a Pseudomonas aeruginosa porin involved in the uptake of tricarboxylates
    • Tamber S, Maier E, Benz R, Hancock RE, (2007) Characterization of OpdH, a Pseudomonas aeruginosa porin involved in the uptake of tricarboxylates. J Bacteriol 189: 929-939.
    • (2007) J Bacteriol , vol.189 , pp. 929-939
    • Tamber, S.1    Maier, E.2    Benz, R.3    Hancock, R.E.4
  • 59
    • 0027318805 scopus 로고
    • Cloning and nucleotide sequence of anaerobically induced porin protein E1 (OprE) of Pseudomonas aeruginosa PAO1
    • Yamano Y, Nishikawa T, Komatsu Y, (1993) Cloning and nucleotide sequence of anaerobically induced porin protein E1 (OprE) of Pseudomonas aeruginosa PAO1. Mol Microbiol 8: 993-1004.
    • (1993) Mol Microbiol , vol.8 , pp. 993-1004
    • Yamano, Y.1    Nishikawa, T.2    Komatsu, Y.3
  • 60
    • 0028037497 scopus 로고
    • Direct measurement of chlorine penetration into biofilms during disinfection
    • de Beer D, Srinivasan R, Stewart PS, (1994) Direct measurement of chlorine penetration into biofilms during disinfection. Appl Environ Microbiol 60: 4339-4344.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4339-4344
    • de Beer, D.1    Srinivasan, R.2    Stewart, P.S.3
  • 61
    • 6444245155 scopus 로고    scopus 로고
    • Anaerobic metabolism and quorum sensing by Pseudomonas aeruginosa biofilms in chronically infected cystic fibrosis airways: rethinking antibiotic treatment strategies and drug targets
    • Hassett DJ, Cuppoletti J, Trapnell B, Lymar SV, Rowe JJ, et al. (2002) Anaerobic metabolism and quorum sensing by Pseudomonas aeruginosa biofilms in chronically infected cystic fibrosis airways: rethinking antibiotic treatment strategies and drug targets. Adv Drug Deliv Rev 54: 1425-1443.
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 1425-1443
    • Hassett, D.J.1    Cuppoletti, J.2    Trapnell, B.3    Lymar, S.V.4    Rowe, J.J.5
  • 62
    • 0031710092 scopus 로고    scopus 로고
    • Spatial physiological heterogeneity in Pseudomonas aeruginosa biofilm is determined by oxygen availability
    • Xu KD, Stewart PS, Xia F, Huang CT, McFeters GA, (1998) Spatial physiological heterogeneity in Pseudomonas aeruginosa biofilm is determined by oxygen availability. Appl Environ Microbiol 64: 4035-4039.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4035-4039
    • Xu, K.D.1    Stewart, P.S.2    Xia, F.3    Huang, C.T.4    McFeters, G.A.5
  • 63
    • 0035023483 scopus 로고    scopus 로고
    • Relevance of microbial extracellular polymeric substances (EPSs) - Part I: Structural and ecological aspects
    • Flemming HC, Wingender J, (2001) Relevance of microbial extracellular polymeric substances (EPSs)- Part I: Structural and ecological aspects. Water Science and Technology 43: 1-8.
    • (2001) Water Science and Technology , vol.43 , pp. 1-8
    • Flemming, H.C.1    Wingender, J.2
  • 65
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B, (2009) Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458: 367-370.
    • (2009) Nature , vol.458 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    van den Berg, B.5
  • 66
    • 0023153689 scopus 로고
    • Purification and characterization of an outer membrane-bound protein involved in long-chain fatty acid transport in Escherichia coli
    • Black PN, Said B, Ghosn CR, Beach JV, Nunn WD, (1987) Purification and characterization of an outer membrane-bound protein involved in long-chain fatty acid transport in Escherichia coli. J Biol Chem 262: 1412-1419.
    • (1987) J Biol Chem , vol.262 , pp. 1412-1419
    • Black, P.N.1    Said, B.2    Ghosn, C.R.3    Beach, J.V.4    Nunn, W.D.5
  • 67
    • 44349103106 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa twitching motility-mediated chemotaxis towards phospholipids and fatty acids: specificity and metabolic requirements
    • Miller RM, Tomaras AP, Barker AP, Voelker DR, Chan ED, et al. (2008) Pseudomonas aeruginosa twitching motility-mediated chemotaxis towards phospholipids and fatty acids: specificity and metabolic requirements. J Bacteriol 190: 4038-4049.
    • (2008) J Bacteriol , vol.190 , pp. 4038-4049
    • Miller, R.M.1    Tomaras, A.P.2    Barker, A.P.3    Voelker, D.R.4    Chan, E.D.5
  • 68
    • 77954373738 scopus 로고    scopus 로고
    • Going forward laterally: transmembrane passage of hydrophobic molecules through protein channel walls
    • van den Berg B, (2010) Going forward laterally: transmembrane passage of hydrophobic molecules through protein channel walls. Chembiochem 11: 1339-1343.
    • (2010) Chembiochem , vol.11 , pp. 1339-1343
    • van den Berg, B.1
  • 69
    • 78149443128 scopus 로고    scopus 로고
    • Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa
    • Kang Y, Zarzycki-Siek J, Walton CB, Norris MH, Hoang TT, (2010) Multiple FadD acyl-CoA synthetases contribute to differential fatty acid degradation and virulence in Pseudomonas aeruginosa. PLoS ONE 5: e13557.
    • (2010) PLoS ONE , vol.5
    • Kang, Y.1    Zarzycki-Siek, J.2    Walton, C.B.3    Norris, M.H.4    Hoang, T.T.5
  • 70
    • 0242654003 scopus 로고    scopus 로고
    • In vitro identification of two adherence factors required for in vivo virulence of Pseudomonas fluorescens
    • de Lima Pimenta A, Di Martino P, Le BE, Hulen C, Blight MA, (2003) In vitro identification of two adherence factors required for in vivo virulence of Pseudomonas fluorescens. Microbes Infect 5: 1177-1187.
    • (2003) Microbes Infect , vol.5 , pp. 1177-1187
    • de Lima Pimenta, A.1    Di Martino, P.2    Le, B.E.3    Hulen, C.4    Blight, M.A.5
  • 71
    • 77954038036 scopus 로고    scopus 로고
    • Molecular mechanisms of ethanol-induced pathogenesis revealed by RNA-sequencing
    • Camarena L, Bruno V, Euskirchen G, Poggio S, Snyder M, (2010) Molecular mechanisms of ethanol-induced pathogenesis revealed by RNA-sequencing. PLoS Pathog 6: e1000834.
    • (2010) PLoS Pathog , vol.6
    • Camarena, L.1    Bruno, V.2    Euskirchen, G.3    Poggio, S.4    Snyder, M.5
  • 72
    • 77951222464 scopus 로고    scopus 로고
    • Inactivation of phospholipase D diminishes Acinetobacter baumannii pathogenesis
    • Jacobs AC, Hood I, Boyd KL, Olson PD, Morrison JM, et al. (2010) Inactivation of phospholipase D diminishes Acinetobacter baumannii pathogenesis. Infect Immun 78: 1952-1962.
    • (2010) Infect Immun , vol.78 , pp. 1952-1962
    • Jacobs, A.C.1    Hood, I.2    Boyd, K.L.3    Olson, P.D.4    Morrison, J.M.5
  • 73
    • 65749117186 scopus 로고    scopus 로고
    • CsuA/BABCDE-dependent pili are not involved in the adherence of Acinetobacter baumannii ATCC19606(T) to human airway epithelial cells and their inflammatory response
    • de Breij A, Gaddy J, van der MJ, Koning R, Koster A, et al. (2009) CsuA/BABCDE-dependent pili are not involved in the adherence of Acinetobacter baumannii ATCC19606(T) to human airway epithelial cells and their inflammatory response. Res Microbiol 160: 213-218.
    • (2009) Res Microbiol , vol.160 , pp. 213-218
    • de Breij, A.1    Gaddy, J.2    van der, M.J.3    Koning, R.4    Koster, A.5
  • 74
    • 33646061665 scopus 로고    scopus 로고
    • Adherence of Acinetobacter baumannii strains to human bronchial epithelial cells
    • Lee JC, Koerten H, van den BP, Beekhuizen H, Wolterbeek R, et al. (2006) Adherence of Acinetobacter baumannii strains to human bronchial epithelial cells. Res Microbiol 157: 360-366.
    • (2006) Res Microbiol , vol.157 , pp. 360-366
    • Lee, J.C.1    Koerten, H.2    van den, B.P.3    Beekhuizen, H.4    Wolterbeek, R.5
  • 75
    • 60149111839 scopus 로고    scopus 로고
    • Pili in Gram-negative and Gram-positive bacteria - structure, assembly and their role in disease
    • Proft T, Baker EN, (2009) Pili in Gram-negative and Gram-positive bacteria- structure, assembly and their role in disease. Cell Mol Life Sci 66: 613-635.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 613-635
    • Proft, T.1    Baker, E.N.2
  • 76
    • 0028831046 scopus 로고
    • Structurally variant classes of pilus appendage fibers coexpressed from Burkholderia (Pseudomonas) cepacia
    • Goldstein R, Sun L, Jiang R, Sajjan U, Forstner JF, et al. (1995) Structurally variant classes of pilus appendage fibers coexpressed from Burkholderia (Pseudomonas) cepacia. J Bacteriol 177: 1039-1052.
    • (1995) J Bacteriol , vol.177 , pp. 1039-1052
    • Goldstein, R.1    Sun, L.2    Jiang, R.3    Sajjan, U.4    Forstner, J.F.5
  • 77
    • 51049118119 scopus 로고    scopus 로고
    • Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria
    • Fronzes R, Remaut H, Waksman G, (2008) Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. EMBO J 27: 2271-2280.
    • (2008) EMBO J , vol.27 , pp. 2271-2280
    • Fronzes, R.1    Remaut, H.2    Waksman, G.3
  • 78
    • 59449102274 scopus 로고    scopus 로고
    • Iron acquisition functions expressed by the human pathogen Acinetobacter baumannii
    • Zimbler DL, Penwell WF, Gaddy JA, Menke SM, Tomaras AP, et al. (2009) Iron acquisition functions expressed by the human pathogen Acinetobacter baumannii. Biometals 22: 23-32.
    • (2009) Biometals , vol.22 , pp. 23-32
    • Zimbler, D.L.1    Penwell, W.F.2    Gaddy, J.A.3    Menke, S.M.4    Tomaras, A.P.5
  • 79
    • 79951852932 scopus 로고    scopus 로고
    • Investigation of the human pathogen Acinetobacter baumannii under iron limiting conditions
    • Eijkelkamp BA, Hassan KA, Paulsen IT, Brown MH, (2011) Investigation of the human pathogen Acinetobacter baumannii under iron limiting conditions. BMC Genomics 12: 126.
    • (2011) BMC Genomics , vol.12 , pp. 126
    • Eijkelkamp, B.A.1    Hassan, K.A.2    Paulsen, I.T.3    Brown, M.H.4
  • 80
    • 22744445608 scopus 로고    scopus 로고
    • Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells
    • Choi CH, Lee EY, Lee YC, Park TI, Kim HJ, et al. (2005) Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells. Cell Microbiol 7: 1127-1138.
    • (2005) Cell Microbiol , vol.7 , pp. 1127-1138
    • Choi, C.H.1    Lee, E.Y.2    Lee, Y.C.3    Park, T.I.4    Kim, H.J.5
  • 81
    • 79952213709 scopus 로고    scopus 로고
    • Acinetobacter baumannii secretes cytotoxic outer membrane protein A via outer membrane vesicles
    • Jin JS, Kwon SO, Moon DC, Gurung M, Lee JH, et al. (2011) Acinetobacter baumannii secretes cytotoxic outer membrane protein A via outer membrane vesicles. PLoS ONE 6: e17027.
    • (2011) PLoS ONE , vol.6
    • Jin, J.S.1    Kwon, S.O.2    Moon, D.C.3    Gurung, M.4    Lee, J.H.5
  • 82
    • 77952357054 scopus 로고    scopus 로고
    • The outer membrane protein OprQ and adherence of Pseudomonas aeruginosa to human fibronectin
    • Arhin A, Boucher C, (2010) The outer membrane protein OprQ and adherence of Pseudomonas aeruginosa to human fibronectin. Microbiology 156: 1415-1423.
    • (2010) Microbiology , vol.156 , pp. 1415-1423
    • Arhin, A.1    Boucher, C.2
  • 83
    • 0036385747 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F is an adhesin in bacterial binding to lung epithelial cells in culture
    • Azghani AO, Idell S, Bains M, Hancock RE, (2002) Pseudomonas aeruginosa outer membrane protein F is an adhesin in bacterial binding to lung epithelial cells in culture. Microb Pathog 33: 109-114.
    • (2002) Microb Pathog , vol.33 , pp. 109-114
    • Azghani, A.O.1    Idell, S.2    Bains, M.3    Hancock, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.