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Volumn 8, Issue 9, 2013, Pages

Systematic Mutational Analysis of the Putative Hydrolase PqsE: Toward a Deeper Molecular Understanding of Virulence Acquisition in Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; BACTERIAL PROTEIN; HYDROLASE; PQSE PROTEIN; UNCLASSIFIED DRUG;

EID: 84883805212     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073727     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 0034890768 scopus 로고    scopus 로고
    • Endemicity, molecular diversity and colonisation routes of Pseudomonas aeruginosa in intensive care units
    • Bertrand X, Thouverez M, Talon D, Boillot A, Capellier G, et al. (2001) Endemicity, molecular diversity and colonisation routes of Pseudomonas aeruginosa in intensive care units. Intensive care medicine 27: 1263-1268.
    • (2001) Intensive Care Medicine , vol.27 , pp. 1263-1268
    • Bertrand, X.1    Thouverez, M.2    Talon, D.3    Boillot, A.4    Capellier, G.5
  • 5
    • 21744449475 scopus 로고    scopus 로고
    • [Epidemiology of nosocomial infections due to Pseudomonas aeruginosa, Burkholderia cepacia and Stenotrophomonas maltophilia]
    • Berthelot P, Grattard F, Mallaval FO, Ros A, Lucht F, et al. (2005) [Epidemiology of nosocomial infections due to Pseudomonas aeruginosa, Burkholderia cepacia and Stenotrophomonas maltophilia]. Pathologie-biologie 53: 341-348.
    • (2005) Pathologie-Biologie , vol.53 , pp. 341-348
    • Berthelot, P.1    Grattard, F.2    Mallaval, F.O.3    Ros, A.4    Lucht, F.5
  • 6
    • 22144494583 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa, Candida albicans, and device-related nosocomial infections: implications, trends, and potential approaches for control
    • Pierce GE, (2005) Pseudomonas aeruginosa, Candida albicans, and device-related nosocomial infections: implications, trends, and potential approaches for control. Journal of industrial microbiology & biotechnology 32: 309-318.
    • (2005) Journal of Industrial Microbiology & Biotechnology , vol.32 , pp. 309-318
    • Pierce, G.E.1
  • 7
    • 33947197663 scopus 로고    scopus 로고
    • The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections
    • Driscoll JA, Brody SL, Kollef MH, (2007) The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections. Drugs 67: 351-368.
    • (2007) Drugs , vol.67 , pp. 351-368
    • Driscoll, J.A.1    Brody, S.L.2    Kollef, M.H.3
  • 8
    • 33846035910 scopus 로고    scopus 로고
    • The role of quorum sensing in the pathogenicity of the cunning aggressor Pseudomonas aeruginosa
    • Bjarnsholt T, Givskov M, (2007) The role of quorum sensing in the pathogenicity of the cunning aggressor Pseudomonas aeruginosa. Analytical and bioanalytical chemistry 387: 409-414.
    • (2007) Analytical and Bioanalytical Chemistry , vol.387 , pp. 409-414
    • Bjarnsholt, T.1    Givskov, M.2
  • 9
    • 63749104134 scopus 로고    scopus 로고
    • Quorum sensing and environmental adaptation in Pseudomonas aeruginosa: a tale of regulatory networks and multifunctional signal molecules
    • Williams P, Camara M, (2009) Quorum sensing and environmental adaptation in Pseudomonas aeruginosa: a tale of regulatory networks and multifunctional signal molecules. Current opinion in microbiology 12: 182-191.
    • (2009) Current Opinion in Microbiology , vol.12 , pp. 182-191
    • Williams, P.1    Camara, M.2
  • 11
    • 14544284036 scopus 로고    scopus 로고
    • The contribution of MvfR to Pseudomonas aeruginosa pathogenesis and quorum sensing circuitry regulation: multiple quorum sensing-regulated genes are modulated without affecting lasRI, rhlRI or the production of N-acyl-L-homoserine lactones
    • Déziel E, Gopalan S, Tampakaki AP, Lépine F, Padfield KE, et al. (2005) The contribution of MvfR to Pseudomonas aeruginosa pathogenesis and quorum sensing circuitry regulation: multiple quorum sensing-regulated genes are modulated without affecting lasRI, rhlRI or the production of N-acyl-L-homoserine lactones. Molecular microbiology 55: 998-1014.
    • (2005) Molecular Microbiology , vol.55 , pp. 998-1014
    • Déziel, E.1    Gopalan, S.2    Tampakaki, A.P.3    Lépine, F.4    Padfield, K.E.5
  • 14
    • 84868112328 scopus 로고    scopus 로고
    • Identification of small-molecule antagonists of the Pseudomonas aeruginosa transcriptional regulator PqsR: biophysically guided hit discovery and optimization
    • Klein T, Henn C, de Jong JC, Zimmer C, Kirsch B, et al. (2012) Identification of small-molecule antagonists of the Pseudomonas aeruginosa transcriptional regulator PqsR: biophysically guided hit discovery and optimization. ACS Chem Biol 7: 1496-1501.
    • (2012) ACS Chem Biol , vol.7 , pp. 1496-1501
    • Klein, T.1    Henn, C.2    de Jong, J.C.3    Zimmer, C.4    Kirsch, B.5
  • 15
    • 84858987560 scopus 로고    scopus 로고
    • Discovery of antagonists of PqsR, a key player in 2-alkyl-4-quinolone-dependent quorum sensing in Pseudomonas aeruginosa
    • Lu C, Kirsch B, Zimmer C, de Jong JC, Henn C, et al. (2012) Discovery of antagonists of PqsR, a key player in 2-alkyl-4-quinolone-dependent quorum sensing in Pseudomonas aeruginosa. Chem Biol 19: 381-390.
    • (2012) Chem Biol , vol.19 , pp. 381-390
    • Lu, C.1    Kirsch, B.2    Zimmer, C.3    de Jong, J.C.4    Henn, C.5
  • 16
    • 84867073873 scopus 로고    scopus 로고
    • Validation of PqsD as an anti-biofilm target in Pseudomonas aeruginosa by development of small-molecule inhibitors
    • Storz MP, Maurer CK, Zimmer C, Wagner N, Brengel C, et al. (2012) Validation of PqsD as an anti-biofilm target in Pseudomonas aeruginosa by development of small-molecule inhibitors. J Am Chem Soc 134: 16143-16146.
    • (2012) J Am Chem Soc , vol.134 , pp. 16143-16146
    • Storz, M.P.1    Maurer, C.K.2    Zimmer, C.3    Wagner, N.4    Brengel, C.5
  • 17
    • 77957967410 scopus 로고    scopus 로고
    • Transcriptomic analysis reveals a global alkyl-quinolone-independent regulatory role for PqsE in facilitating the environmental adaptation of Pseudomonas aeruginosa to plant and animal hosts
    • Rampioni G, Pustelny C, Fletcher MP, Wright VJ, Bruce M, et al. (2010) Transcriptomic analysis reveals a global alkyl-quinolone-independent regulatory role for PqsE in facilitating the environmental adaptation of Pseudomonas aeruginosa to plant and animal hosts. Environmental microbiology 12: 1659-1673.
    • (2010) Environmental Microbiology , vol.12 , pp. 1659-1673
    • Rampioni, G.1    Pustelny, C.2    Fletcher, M.P.3    Wright, V.J.4    Bruce, M.5
  • 18
    • 77950400018 scopus 로고    scopus 로고
    • Homeostatic interplay between bacterial cell-cell signaling and iron in virulence
    • Hazan R, He J, Xiao G, Dekimpe V, Apidianakis Y, et al. (2010) Homeostatic interplay between bacterial cell-cell signaling and iron in virulence. PLoS Pathogens 6: e1000810.
    • (2010) PLoS Pathogens , vol.6
    • Hazan, R.1    He, J.2    Xiao, G.3    Dekimpe, V.4    Apidianakis, Y.5
  • 19
    • 55749096264 scopus 로고    scopus 로고
    • PqsE functions independently of PqsR-Pseudomonas quinolone signal and enhances the rhl quorum-sensing system
    • Farrow JM, (2008) PqsE functions independently of PqsR-Pseudomonas quinolone signal and enhances the rhl quorum-sensing system. Journal of bacteriology 190: 7043-7051.
    • (2008) Journal of Bacteriology , vol.190 , pp. 7043-7051
    • Farrow, J.M.1
  • 20
    • 70350495852 scopus 로고    scopus 로고
    • Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein
    • Yu S, Jensen V, Seeliger J, Feldmann I, Weber S, et al. (2009) Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry 48: 10298-10307.
    • (2009) Biochemistry , vol.48 , pp. 10298-10307
    • Yu, S.1    Jensen, V.2    Seeliger, J.3    Feldmann, I.4    Weber, S.5
  • 21
    • 70349847872 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0
    • Dehouck Y, Grosfils A, Folch B, Gilis D, Bogaerts P, et al. (2009) Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0. Bioinformatics 25: 2537-2543.
    • (2009) Bioinformatics , vol.25 , pp. 2537-2543
    • Dehouck, Y.1    Grosfils, A.2    Folch, B.3    Gilis, D.4    Bogaerts, P.5
  • 23
    • 0025117531 scopus 로고
    • Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications
    • Essar DW, Eberly L, Hadero A, Crawford IP, (1990) Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications. Journal of bacteriology 172: 884-900.
    • (1990) Journal of Bacteriology , vol.172 , pp. 884-900
    • Essar, D.W.1    Eberly, L.2    Hadero, A.3    Crawford, I.P.4
  • 24
    • 33746257392 scopus 로고    scopus 로고
    • Functional genetic analysis reveals a 2-alkyl-4-quinolone signaling system in the human pathogen Burkholderia pseudomallei and related bacteria
    • Diggle SP, Lumjiaktase P, Dipilato F, Winzer K, Kunakorn M, et al. (2006) Functional genetic analysis reveals a 2-alkyl-4-quinolone signaling system in the human pathogen Burkholderia pseudomallei and related bacteria. Chem Biol 13: 701-710.
    • (2006) Chem Biol , vol.13 , pp. 701-710
    • Diggle, S.P.1    Lumjiaktase, P.2    Dipilato, F.3    Winzer, K.4    Kunakorn, M.5
  • 25
    • 48149111001 scopus 로고    scopus 로고
    • Ambifaria produce 4-hydroxy-2-alkylquinoline analogues with a methyl group at the 3 position that is required for quorum-sensing regulation
    • Burkholderia pseudomallei, B. thailandensis, and B
    • Vial L, Lépine F, Milot S, Groleau MC, Dekimpe V, et al. (2008) Burkholderia pseudomallei, B. thailandensis, and B. ambifaria produce 4-hydroxy-2-alkylquinoline analogues with a methyl group at the 3 position that is required for quorum-sensing regulation. J Bacteriol 190: 5339-5352.
    • (2008) J Bacteriol , vol.190 , pp. 5339-5352
    • Vial, L.1    Lépine, F.2    Milot, S.3    Groleau, M.C.4    Dekimpe, V.5
  • 27
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C, (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 28
    • 33747829924 scopus 로고    scopus 로고
    • Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee
    • Armougom F, Moretti S, Poirot O, Audic S, Dumas P, et al. (2006) Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic acids research 34: W604-608.
    • (2006) Nucleic Acids Research , vol.34
    • Armougom, F.1    Moretti, S.2    Poirot, O.3    Audic, S.4    Dumas, P.5
  • 29
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold
    • Daiyasu H, Osaka K, Ishino Y, Toh H, (2001) Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS letters 503: 1-6.
    • (2001) FEBS Letters , vol.503 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 31
    • 3543143812 scopus 로고    scopus 로고
    • Integrating protein secondary structure prediction and multiple sequence alignment
    • Simossis VA, Heringa J, (2004) Integrating protein secondary structure prediction and multiple sequence alignment. Curr Protein Pept Sci 5: 249-266.
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 249-266
    • Simossis, V.A.1    Heringa, J.2
  • 32
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde R, Edwards L, Regan L, (2008) Structure and function of KH domains. FEBS J 275: 2712-2726.
    • (2008) FEBS J , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 33
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0030777760 scopus 로고    scopus 로고
    • Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence
    • Gilis D, Rooman M, (1997) Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence. J Mol Biol 272: 276-290.
    • (1997) J Mol Biol , vol.272 , pp. 276-290
    • Gilis, D.1    Rooman, M.2
  • 36
    • 0033531792 scopus 로고    scopus 로고
    • Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism
    • Paul-Soto R, Bauer R, Frere JM, Galleni M, Meyer-Klaucke W, et al. (1999) Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism. J Biol Chem 274: 13242-13249.
    • (1999) J Biol Chem , vol.274 , pp. 13242-13249
    • Paul-Soto, R.1    Bauer, R.2    Frere, J.M.3    Galleni, M.4    Meyer-Klaucke, W.5
  • 37
    • 0031728459 scopus 로고    scopus 로고
    • A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases
    • Melino S, Capo C, Dragani B, Aceto A, Petruzzelli R, (1998) A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases. Trends Biochem Sci 23: 381-382.
    • (1998) Trends Biochem Sci , vol.23 , pp. 381-382
    • Melino, S.1    Capo, C.2    Dragani, B.3    Aceto, A.4    Petruzzelli, R.5
  • 38
    • 11244317355 scopus 로고    scopus 로고
    • Metallo-beta-lactamases: two binding sites for one catalytic metal ion?
    • Heinz U, Adolph HW, (2004) Metallo-beta-lactamases: two binding sites for one catalytic metal ion? Cell Mol Life Sci 61: 2827-2839.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2827-2839
    • Heinz, U.1    Adolph, H.W.2
  • 39
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi A, Pares S, Duee E, Galleni M, Duez C, et al. (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14: 4914-4921.
    • (1995) EMBO J , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duee, E.3    Galleni, M.4    Duez, C.5
  • 40
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis
    • Concha NO, Rasmussen BA, Bush K, Herzberg O, (1996) Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure 4: 823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 41
    • 0036566439 scopus 로고    scopus 로고
    • Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase
    • de Seny D, Prosperi-Meys C, Bebrone C, Rossolini GM, Page MI, et al. (2002) Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-beta-lactamase. Biochem J 363: 687-696.
    • (2002) Biochem J , vol.363 , pp. 687-696
    • de Seny, D.1    Prosperi-Meys, C.2    Bebrone, C.3    Rossolini, G.M.4    Page, M.I.5
  • 42
    • 77955860301 scopus 로고    scopus 로고
    • The first crystal structure of an archaeal metallo-beta-lactamase superfamily protein; ST1585 from Sulfolobus tokodaii
    • Shimada A, Ishikawa H, Nakagawa N, Kuramitsu S, Masui R, (2010) The first crystal structure of an archaeal metallo-beta-lactamase superfamily protein; ST1585 from Sulfolobus tokodaii. Proteins 78: 2399-2402.
    • (2010) Proteins , vol.78 , pp. 2399-2402
    • Shimada, A.1    Ishikawa, H.2    Nakagawa, N.3    Kuramitsu, S.4    Masui, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.