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Volumn 50, Issue 5, 2006, Pages 1780-1787

Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level β-lactam resistance involves three AmpD homologues

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE AMPC; CEFOXITIN; CEFTAZIDIME; CEPHALOSPORIN DERIVATIVE; CEPHALOSPORINASE; IMIPENEM; MUTANT PROTEIN; PENICILLIN DERIVATIVE; PIPERACILLIN; PROTEIN AMPD; PROTEIN AMPDH3; TICARCILLIN; UNCLASSIFIED DRUG;

EID: 33646458074     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.50.5.1780-1787.2006     Document Type: Article
Times cited : (144)

References (43)
  • 1
    • 0036841078 scopus 로고    scopus 로고
    • Constitutive high expression of chromosomal β-lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampD
    • Bagge, N., O. Ciofu, M. Hentzer, J. I. A. Campbell, M. Givskov, and N. Hoiby. 2002. Constitutive high expression of chromosomal β-lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampD. Antimicrob. Agents Chemother. 46:3406-3411.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3406-3411
    • Bagge, N.1    Ciofu, O.2    Hentzer, M.3    Campbell, J.I.A.4    Givskov, M.5    Hoiby, N.6
  • 2
    • 1642543160 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa biofilms exposed to imipenem exhibit changes in global gene expression and β-lactamase and alginate production
    • Bagge, N., M. Schuster, M. Morten, O. Ciofu, M. Givskov, E. P. Greenberg, and N. Hoiby. 2004. Pseudomonas aeruginosa biofilms exposed to imipenem exhibit changes in global gene expression and β-lactamase and alginate production. Antimicrob. Agents Chemother. 48:1175-1187.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1175-1187
    • Bagge, N.1    Schuster, M.2    Morten, M.3    Ciofu, O.4    Givskov, M.5    Greenberg, E.P.6    Hoiby, N.7
  • 3
    • 0000182975 scopus 로고
    • XL1 Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection
    • Bullock, W. O., J. M. Fernandez, and J. M. Short. 1987. XL1 Blue: a high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection. BioTechniques 5:376-378.
    • (1987) BioTechniques , vol.5 , pp. 376-378
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 4
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 5
    • 0033059706 scopus 로고    scopus 로고
    • Emergence of antibiotic-resistant Pseudomonas aeruginosa: Comparison of risk associated with different antipseudomonal agents
    • Carmeli, Y., N. Troillet, G. M. Eliopoulos, and M. S. Samore. 1999. Emergence of antibiotic-resistant Pseudomonas aeruginosa: comparison of risk associated with different antipseudomonal agents. Antimicrob. Agents Chemother. 43:1379-1382.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1379-1382
    • Carmeli, Y.1    Troillet, N.2    Eliopoulos, G.M.3    Samore, M.S.4
  • 7
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl-penta-peptide
    • Dietz, H., D. Pfeifle, and B. Wiedemann. 1997. The signal molecule for β-lactamase induction in Enterobacter cloacae is the anhydromuramyl-penta- peptide. Antimicrob. Agents Chemother. 41:2113-2120.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 8
    • 0029057714 scopus 로고
    • Development of resistance during antimicrobial therapy: A review of antibiotic classes and patient characteristics in 173 studies
    • Fish, D. N., S. C. Piscitelli, and L. H. Danziger. 1995. Development of resistance during antimicrobial therapy: a review of antibiotic classes and patient characteristics in 173 studies. Pharmacotherapy 15:279-291.
    • (1995) Pharmacotherapy , vol.15 , pp. 279-291
    • Fish, D.N.1    Piscitelli, S.C.2    Danziger, L.H.3
  • 9
    • 12444260805 scopus 로고    scopus 로고
    • Components of the peptidoglycan-recycling pathway modulate invasion and intracellular survival of Salmonella enterica serovar Typhimurium
    • Folkesson, F., S. Eriksson, M. Andersson, J. T. Park, and S. Normark. 2005. Components of the peptidoglycan-recycling pathway modulate invasion and intracellular survival of Salmonella enterica serovar Typhimurium. Cell. Microbiol. 7:147-155.
    • (2005) Cell. Microbiol. , vol.7 , pp. 147-155
    • Folkesson, F.1    Eriksson, S.2    Andersson, M.3    Park, J.T.4    Normark, S.5
  • 10
    • 1642535322 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic centre of the Citrobacter freundii AmpD N-acetylmuramyl-L-alanine amidase
    • Généreux, C., D. Dehareng, B. Devreese, J. van Beeumen, J. M. Frère, and B. Joris. 2004. Mutational analysis of the catalytic centre of the Citrobacter freundii AmpD N-acetylmuramyl-L-alanine amidase. Biochem. J. 377:111-120.
    • (2004) Biochem. J. , vol.377 , pp. 111-120
    • Généreux, C.1    Dehareng, D.2    Devreese, B.3    Van Beeumen, J.4    Frère, J.M.5    Joris, B.6
  • 11
    • 2542479978 scopus 로고    scopus 로고
    • Biochemical characterization of the naturally occurring oxacillinase OXA-50 of Pseudomonas aeruginosa
    • Girlich, D., T. Naas, and P. Nordmann. 2004. Biochemical characterization of the naturally occurring oxacillinase OXA-50 of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 48:2043-2048.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2043-2048
    • Girlich, D.1    Naas, T.2    Nordmann, P.3
  • 12
    • 0025061590 scopus 로고
    • Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed β-lactamase producing strains
    • Giwercman, B., P. A. Lambert, V. T. Rosdahl, G. H. Shand, and N. Hoiby. 1990. Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed β-lactamase producing strains. J. Antimicrob. Chemother. 26:247-259.
    • (1990) J. Antimicrob. Chemother. , vol.26 , pp. 247-259
    • Giwercman, B.1    Lambert, P.A.2    Rosdahl, V.T.3    Shand, G.H.4    Hoiby, N.5
  • 13
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan, J. R., and V. Deretic. 1996. Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol. Rev. 60:539-574.
    • (1996) Microbiol. Rev. , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 14
    • 0028168986 scopus 로고
    • The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase
    • Höltje, J. V., U. Kopp, A. Ursinus, and B. Wiedemann. 1994. The negative regulator of β-lactamase induction AmpD is a N-acetyl- anhydromuramyl-L-alanine amidase. FEMS Microbiol. Lett. 122:159-164.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 159-164
    • Höltje, J.V.1    Kopp, U.2    Ursinus, A.3    Wiedemann, B.4
  • 15
    • 0023054166 scopus 로고
    • Inducible cephalosporinase production in clinical isolates of Enterobacter cloacae is controlled by a regulatory gene that has been deleted from Escherichia coli
    • Honore, N., M. H. Nicolas, and S. T. Cole. 1986. Inducible cephalosporinase production in clinical isolates of Enterobacter cloacae is controlled by a regulatory gene that has been deleted from Escherichia coli. EMBO J. 5:3709-3714.
    • (1986) EMBO J. , vol.5 , pp. 3709-3714
    • Honore, N.1    Nicolas, M.H.2    Cole, S.T.3
  • 16
    • 0024383568 scopus 로고
    • Regulation of enterobacterial cephalosporinase production: The role of a membrane-bound sensory transducer
    • Honore, N., M. H. Nicolas, and S. T. Cole. 1989. Regulation of enterobacterial cephalosporinase production: the role of a membrane-bound sensory transducer. Mol. Microbiol. 3:1121-1130.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1121-1130
    • Honore, N.1    Nicolas, M.H.2    Cole, S.T.3
  • 17
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs, C., L. Huang, E. Bartowsky, S. Normark, and J. T. Park. 1994. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction. EMBO J. 13:4684-4694.
    • (1994) EMBO J. , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 18
    • 27544473088 scopus 로고    scopus 로고
    • Contribution of clonal dissemination and selection of mutants during therapy to Pseudomonas aeruginosa antimicrobial resistance in an intensive care unit setting
    • Juan, C., O. Gutiérrez, A. Oliver, J. I. Ayestarán, N. Borrell, and J. L. Pérez. 2005. Contribution of clonal dissemination and selection of mutants during therapy to Pseudomonas aeruginosa antimicrobial resistance in an intensive care unit setting. Clin. Microbiol. Infect. 11:887-892.
    • (2005) Clin. Microbiol. Infect. , vol.11 , pp. 887-892
    • Juan, C.1    Gutiérrez, O.2    Oliver, A.3    Ayestarán, J.I.4    Borrell, N.5    Pérez, J.L.6
  • 19
    • 27644573842 scopus 로고    scopus 로고
    • Molecular mechanisms of β-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains
    • Juan, C., M. D. Maciá, O. Gutiérrez, C. Vidal, J. L. Pérez, and A. Oliver. 2005. Molecular mechanisms of β-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 49:4733-4738.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4733-4738
    • Juan, C.1    Maciá, M.D.2    Gutiérrez, O.3    Vidal, C.4    Pérez, J.L.5    Oliver, A.6
  • 21
    • 27644463418 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors
    • Kong, K. F., S. R. Jayawardena, S. D. Indulkar, A. del Puerto, C. L. Koh, N. Hoiby, and K. Mathee. 2005. Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB β-lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob. Agents Chemother. 49:4567-4575.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4567-4575
    • Kong, K.F.1    Jayawardena, S.R.2    Indulkar, S.D.3    Del Puerto, A.4    Koh, C.L.5    Hoiby, N.6    Mathee, K.7
  • 22
    • 0024469170 scopus 로고
    • ampG is essential for high-level expression of AmpC β-lactamase in Enterobacter cloacae
    • Korfmann, G., and C. C. Sanders. 1989. ampG is essential for high-level expression of AmpC β-lactamase in Enterobacter cloacae. Antimicrob. Agents Chemother. 33:1946-1951.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1946-1951
    • Korfmann, G.1    Sanders, C.C.2
  • 23
    • 0031760856 scopus 로고    scopus 로고
    • An ampD gene of Pseudomonas aeruginosa encodes a negative regulator of AmpC β-lactamase expression
    • Langaee, T. Y., M. Dargis, and A. Huletsky. 1998. An ampD gene of Pseudomonas aeruginosa encodes a negative regulator of AmpC β-lactamase expression. Antimicrob. Agents Chemother. 42:3296-3300.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 3296-3300
    • Langaee, T.Y.1    Dargis, M.2    Huletsky, A.3
  • 24
    • 0033993765 scopus 로고    scopus 로고
    • Inactivation of the ampD gene in Pseudomonas aeruginosa leads to moderate-basal-level and hyper-inducible AmpC β-lactamase expression
    • Langaee, T. Y., L. Gagnon, and A. Huletsky. 2000. Inactivation of the ampD gene in Pseudomonas aeruginosa leads to moderate-basal-level and hyper-inducible AmpC β-lactamase expression. Antimicrob. Agents Chemother. 44:583-589.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 583-589
    • Langaee, T.Y.1    Gagnon, L.2    Huletsky, A.3
  • 25
    • 0000623780 scopus 로고
    • Regulatory components in Citrobacter freundii ampC β-lactamase induction
    • Lindberg, F., L. Westman, and S. Normark. 1985. Regulatory components in Citrobacter freundii ampC β-lactamase induction. Proc. Natl. Acad. Sci. USA 82:4620-4624.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4620-4624
    • Lindberg, F.1    Westman, L.2    Normark, S.3
  • 26
    • 0023216969 scopus 로고
    • Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii β-lactamase
    • Lindberg, F., S. Lindquist, and S. Normark. 1987. Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii β-lactamase. J. Bacteriol. 169:1923-1928.
    • (1987) J. Bacteriol. , vol.169 , pp. 1923-1928
    • Lindberg, F.1    Lindquist, S.2    Normark, S.3
  • 27
    • 0023583815 scopus 로고
    • Clinical significance of β-lactamase induction and stable derepression in gram-negative rods
    • Livermore, D. M. 1987. Clinical significance of β-lactamase induction and stable derepression in gram-negative rods. Eur. J. Clin. Microbiol. 6:439-445.
    • (1987) Eur. J. Clin. Microbiol. , vol.6 , pp. 439-445
    • Livermore, D.M.1
  • 28
    • 0028883511 scopus 로고
    • β-lactamases in laboratory and clinical resistance
    • Livermore, D. M. 1995. β-Lactamases in laboratory and clinical resistance. Clin. Microbiol. Rev. 8:557-584.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 29
  • 30
    • 0036498656 scopus 로고    scopus 로고
    • Multiple mechanisms of antimicrobial resistance in Pseudomonas aeruginosa: Our worst nightmare?
    • Livermore, D. M. 2002. Multiple mechanisms of antimicrobial resistance in Pseudomonas aeruginosa: our worst nightmare? Clin. Infect. Dis. 34:634-640.
    • (2002) Clin. Infect. Dis. , vol.34 , pp. 634-640
    • Livermore, D.M.1
  • 31
    • 0027328960 scopus 로고
    • Investigation of the Pseudomonas aeruginosa ampR gene and its role at the chromosomal ampC promoter
    • Lodge, J., S. Busby, and L. Piddock. 1993. Investigation of the Pseudomonas aeruginosa ampR gene and its role at the chromosomal ampC promoter. FEMS Microbiol. Lett. 111:315-320.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 315-320
    • Lodge, J.1    Busby, S.2    Piddock, L.3
  • 32
    • 0036841380 scopus 로고    scopus 로고
    • Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria
    • Marx, C. J., and M. E. Lidstrom. 2002. Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria. BioTechniques 33:1062-1067.
    • (2002) BioTechniques , vol.33 , pp. 1062-1067
    • Marx, C.J.1    Lidstrom, M.E.2
  • 33
    • 0029311691 scopus 로고
    • β-lactamase induction in gram-negative bacteria is intimately linked to peptidoglycan recycling
    • Normark, S. 1995. β-Lactamase induction in gram-negative bacteria is intimately linked to peptidoglycan recycling. Microb. Drug Resist. 1:111-114.
    • (1995) Microb. Drug Resist. , vol.1 , pp. 111-114
    • Normark, S.1
  • 34
    • 0033901763 scopus 로고    scopus 로고
    • Inactivation of the ampDE operon increases transcription of algD and affects morphology and encystment of Azotobacter vinelandii
    • Nuñez, C., S. Moreno, L. Cárdenas, G. Soberón-Chavez, and G, Espín. 2000. Inactivation of the ampDE operon increases transcription of algD and affects morphology and encystment of Azotobacter vinelandii. J. Bacteriol. 182:4829-4835.
    • (2000) J. Bacteriol. , vol.182 , pp. 4829-4835
    • Nuñez, C.1    Moreno, S.2    Cárdenas, L.3    Soberón-Chavez, G.4    Espín, G.5
  • 35
    • 0842307683 scopus 로고    scopus 로고
    • Role of efflux pumps and mutations in genes for topoisomerases II and IV in fluoroquinolone-resistant Pseudomonas aeruginosa strains
    • Oh, H., J. Stenhoff, S. Jalal, and B. Wretlind. 2003. Role of efflux pumps and mutations in genes for topoisomerases II and IV in fluoroquinolone-resistant Pseudomonas aeruginosa strains. Microb. Drug Resist. 8:323-328.
    • (2003) Microb. Drug Resist. , vol.8 , pp. 323-328
    • Oh, H.1    Stenhoff, J.2    Jalal, S.3    Wretlind, B.4
  • 36
    • 0034685940 scopus 로고    scopus 로고
    • High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection
    • Oliver, A., R. Cantón, P. Campo, F. Baquero, and J. Blázquez. 2000. High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288:1251-1253.
    • (2000) Science , vol.288 , pp. 1251-1253
    • Oliver, A.1    Cantón, R.2    Campo, P.3    Baquero, F.4    Blázquez, J.5
  • 37
    • 12344249544 scopus 로고    scopus 로고
    • Combined sacB-based negative selection and cre-lox antibiotic marker recycling for efficient gene deletion in Pseudomonas aeruginosa
    • Quénée, L., D. Lamotte, and B. Polack. 2005. Combined sacB-based negative selection and cre-lox antibiotic marker recycling for efficient gene deletion in Pseudomonas aeruginosa. BioTechniques 38:63-67.
    • (2005) BioTechniques , vol.38 , pp. 63-67
    • Quénée, L.1    Lamotte, D.2    Polack, B.3
  • 38
    • 0021027842 scopus 로고
    • A broad range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad 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
  • 39
    • 0024787898 scopus 로고
    • Transformation of Pseudomonas aeruginosa by electroporation
    • Smith, A. W., and B. H. Iglewski. 1989. Transformation of Pseudomonas aeruginosa by electroporation. Nucleic Acids Res. 17:10509.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10509
    • Smith, A.W.1    Iglewski, B.H.2
  • 40
    • 0028835130 scopus 로고
    • DNA sequence differences of ampD mutants of Citrobacter freundii
    • Stapleton, P., K. Shannon, and I. Phillips. 1995. DNA sequence differences of ampD mutants of Citrobacter freundii. Antimicrob. Agents Chemother. 39:2494-2498.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2494-2498
    • Stapleton, P.1    Shannon, K.2    Phillips, I.3
  • 42
    • 0038177618 scopus 로고    scopus 로고
    • Nosocomial infections in adult intensive-care units
    • Vincent, J. L. 2003. Nosocomial infections in adult intensive-care units. Lancet 361:2068-2077.
    • (2003) Lancet , vol.361 , pp. 2068-2077
    • Vincent, J.L.1
  • 43
    • 0028172499 scopus 로고
    • Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa
    • West, S. E., H. P. Schweizer, C. Dall, A. K. Sample, and L. J. Runyen-Janecky. 1994. Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa. Gene 148:81-86.
    • (1994) Gene , vol.148 , pp. 81-86
    • West, S.E.1    Schweizer, H.P.2    Dall, C.3    Sample, A.K.4    Runyen-Janecky, L.J.5


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