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Volumn 35, Issue 3, 2010, Pages 244-249

Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to β-lactam agents

Author keywords

Lactam sensitivity; Escherichia coli; Penicillin binding protein

Indexed keywords

AMOXICILLIN; AMPICILLIN; BACTERIAL PROTEIN; BETA LACTAM ANTIBIOTIC; CEFACLOR; CEFADROXIL; CEFALEXIN; CEFALOTIN; CEPHALOSPORIN DERIVATIVE; CHLORAMPHENICOL; KANAMYCIN; NITROCEFIN; O ANTIGEN; PENICILLIN BINDING PROTEIN 5; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; PROTEIN DACA; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 73549109625     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijantimicag.2009.11.004     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis
    • Denome S.A., Elf P.K., Henderson T.A., Nelson D.E., and Young K.D. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J Bacteriol 181 (1999) 3981-3993
    • (1999) J Bacteriol , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 2
    • 0034006505 scopus 로고    scopus 로고
    • Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli
    • Nelson D.E., and Young K.D. Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. J Bacteriol 182 (2000) 1714-1721
    • (2000) J Bacteriol , vol.182 , pp. 1714-1721
    • Nelson, D.E.1    Young, K.D.2
  • 3
    • 0035026549 scopus 로고    scopus 로고
    • Contributions of PBP5 and dd-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli
    • Nelson D.E., and Young K.D. Contributions of PBP5 and dd-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli. J Bacteriol 183 (2001) 3055-3064
    • (2001) J Bacteriol , vol.183 , pp. 3055-3064
    • Nelson, D.E.1    Young, K.D.2
  • 4
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • Dougherty T.J., Kennedy K., Kessler R.E., and Pucci M.J. Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J Bacteriol 178 (1996) 6110-6115
    • (1996) J Bacteriol , vol.178 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 5
    • 46249130782 scopus 로고    scopus 로고
    • Physiological functions of d-alanine carboxypeptidases in Escherichia coli
    • Ghosh A.S., Chowdhury C., and Nelson D.E. Physiological functions of d-alanine carboxypeptidases in Escherichia coli. Trends Microbiol 16 (2008) 309-317
    • (2008) Trends Microbiol , vol.16 , pp. 309-317
    • Ghosh, A.S.1    Chowdhury, C.2    Nelson, D.E.3
  • 6
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje J.V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62 (1998) 181-183
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-183
    • Holtje, J.V.1
  • 7
    • 0023865255 scopus 로고
    • Hybrid penicillin-binding proteins in penicillin-resistant strains of Neisseria gonorrhoeae
    • Spratt B.G. Hybrid penicillin-binding proteins in penicillin-resistant strains of Neisseria gonorrhoeae. Nature 332 (1988) 173-176
    • (1988) Nature , vol.332 , pp. 173-176
    • Spratt, B.G.1
  • 8
    • 0033194691 scopus 로고    scopus 로고
    • Different penicillin-binding protein profiles in amoxicillin-resistant Helicobacter pylori
    • Dore M.P., Graham D.Y., and Sepulveda A.R. Different penicillin-binding protein profiles in amoxicillin-resistant Helicobacter pylori. Helicobacter 4 (1999) 154-161
    • (1999) Helicobacter , vol.4 , pp. 154-161
    • Dore, M.P.1    Graham, D.Y.2    Sepulveda, A.R.3
  • 9
    • 33646701915 scopus 로고    scopus 로고
    • Multiple mutations in or adjacent to the conserved penicillin-binding protein motifs of the penicillin-binding protein 1A confer amoxicillin resistance to Helicobacter pylori
    • Gerrits M.M., Godoy A.P., Kuipers E.J., Ribeiro M.L., Stoof J., Mendonca S., et al. Multiple mutations in or adjacent to the conserved penicillin-binding protein motifs of the penicillin-binding protein 1A confer amoxicillin resistance to Helicobacter pylori. Helicobacter 11 (2006) 181-187
    • (2006) Helicobacter , vol.11 , pp. 181-187
    • Gerrits, M.M.1    Godoy, A.P.2    Kuipers, E.J.3    Ribeiro, M.L.4    Stoof, J.5    Mendonca, S.6
  • 10
    • 0025284661 scopus 로고
    • Resistance of Pseudomonas aeruginosa to cefsulodin: modification of penicillin-binding protein 3 and mapping of its chromosomal gene
    • Gotoh N., Nunomura K., and Nishino T. Resistance of Pseudomonas aeruginosa to cefsulodin: modification of penicillin-binding protein 3 and mapping of its chromosomal gene. J Antimicrob Chemother 25 (1990) 513-523
    • (1990) J Antimicrob Chemother , vol.25 , pp. 513-523
    • Gotoh, N.1    Nunomura, K.2    Nishino, T.3
  • 11
    • 0032581405 scopus 로고    scopus 로고
    • Alterations in high molecular mass penicillin-binding protein 1 associated with β-lactam resistance in Shigella dysenteriae
    • Ghosh A.S., Kar A.K., and Kundu M. Alterations in high molecular mass penicillin-binding protein 1 associated with β-lactam resistance in Shigella dysenteriae. Biochem Biophys Res Commun 248 (1998) 669-672
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 669-672
    • Ghosh, A.S.1    Kar, A.K.2    Kundu, M.3
  • 12
    • 0036171501 scopus 로고    scopus 로고
    • Mutations in ponA, the gene encoding penicillin-binding protein 1, and a novel locus, penC, are required for high-level chromosomally mediated penicillin resistance in Neisseria gonorrhoeae
    • Ropp P.A., Hu M., Olesky M., and Nicholas R.A. Mutations in ponA, the gene encoding penicillin-binding protein 1, and a novel locus, penC, are required for high-level chromosomally mediated penicillin resistance in Neisseria gonorrhoeae. Antimicrob Agents Chemother 46 (2002) 769-777
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 769-777
    • Ropp, P.A.1    Hu, M.2    Olesky, M.3    Nicholas, R.A.4
  • 13
    • 0024331495 scopus 로고
    • Recruitment of a penicillin-binding protein gene from Neisseria flavescens during the emergence of penicillin resistance in Neisseria meningitidis
    • Spratt B.G., Zhang Q.Y., Jones D.M., Hutchison A., Brannigan J.A., and Dowson C.G. Recruitment of a penicillin-binding protein gene from Neisseria flavescens during the emergence of penicillin resistance in Neisseria meningitidis. Proc Natl Acad Sci USA 86 (1989) 8988-8992
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8988-8992
    • Spratt, B.G.1    Zhang, Q.Y.2    Jones, D.M.3    Hutchison, A.4    Brannigan, J.A.5    Dowson, C.G.6
  • 14
    • 63449128597 scopus 로고    scopus 로고
    • β-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein
    • Moya B., Dotsch A., Juan C., Blazquez J., Zamorano L., Haussler S., et al. β-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. PLoS Pathog 5 (2009) e1000353
    • (2009) PLoS Pathog , vol.5
    • Moya, B.1    Dotsch, A.2    Juan, C.3    Blazquez, J.4    Zamorano, L.5    Haussler, S.6
  • 15
    • 41549090908 scopus 로고    scopus 로고
    • Involvement of O8-antigen in altering β-lactam antibiotic susceptibilities in Escherichia coli
    • Sarkar S.K., and Ghosh A.S. Involvement of O8-antigen in altering β-lactam antibiotic susceptibilities in Escherichia coli. FEMS Microbiol Lett 282 (2008) 59-64
    • (2008) FEMS Microbiol Lett , vol.282 , pp. 59-64
    • Sarkar, S.K.1    Ghosh, A.S.2
  • 16
    • 3142671582 scopus 로고    scopus 로고
    • Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coli
    • Nilsen T., Ghosh A.S., Goldberg M.B., and Young K.D. Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coli. Mol Microbiol 52 (2004) 1045-1054
    • (2004) Mol Microbiol , vol.52 , pp. 1045-1054
    • Nilsen, T.1    Ghosh, A.S.2    Goldberg, M.B.3    Young, K.D.4
  • 17
    • 0037378572 scopus 로고    scopus 로고
    • Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli
    • Ghosh A.S., and Young K.D. Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli. J Bacteriol 185 (2003) 2178-2186
    • (2003) J Bacteriol , vol.185 , pp. 2178-2186
    • Ghosh, A.S.1    Young, K.D.2
  • 18
    • 0028896922 scopus 로고
    • Site-specific deletions of chromosomally located DNA segments with the multimer resolution system of broad-host-range plasmid RP4
    • Kristensen C.S., Eberl L., Sanchez-Romero J.M., Givskov M., Molin S., and De Lorenzo V. Site-specific deletions of chromosomally located DNA segments with the multimer resolution system of broad-host-range plasmid RP4. J Bacteriol 177 (1995) 52-58
    • (1995) J Bacteriol , vol.177 , pp. 52-58
    • Kristensen, C.S.1    Eberl, L.2    Sanchez-Romero, J.M.3    Givskov, M.4    Molin, S.5    De Lorenzo, V.6
  • 19
    • 0032908481 scopus 로고    scopus 로고
    • Bocillin FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • Zhao G., Meier T.I., Kahl S.D., Gee K.R., and Blaszczak L.C. Bocillin FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob Agents Chemother 43 (1999) 1124-1128
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5
  • 20
    • 34948893943 scopus 로고    scopus 로고
    • Performance standards for antimicrobial susceptibility testing
    • Clinical and Laboratory Standards Institute
    • Clinical and Laboratory Standards Institute. Performance standards for antimicrobial susceptibility testing. Seventeenth informational supplement. Document M100-S17. CLSI, Wayne, PA: CLSI; 2007.
    • (2007) Seventeenth informational supplement. Document M100-S17. CLSI, Wayne, PA: CLSI
  • 21
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance
    • Stubbs K.A., Balcewich M., Mark B.L., and Vocadlo D.J. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance. J Biol Chem 282 (2007) 21382-21391
    • (2007) J Biol Chem , vol.282 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 22
    • 0033031973 scopus 로고    scopus 로고
    • Impaired imipenem uptake associated with alterations in outer membrane proteins and lipopolysaccharides in imipenem-resistant Shigella dysenteriae
    • Ghosh A.S., Kar A.K., and Kundu M. Impaired imipenem uptake associated with alterations in outer membrane proteins and lipopolysaccharides in imipenem-resistant Shigella dysenteriae. J Antimicrob Chemother 43 (1999) 195-201
    • (1999) J Antimicrob Chemother , vol.43 , pp. 195-201
    • Ghosh, A.S.1    Kar, A.K.2    Kundu, M.3
  • 23
    • 0023878451 scopus 로고
    • Site-directed mutants of a soluble form of penicillin-binding protein 5 from Escherichia coli and their catalytic properties
    • Nicholas R.A., and Strominger J.L. Site-directed mutants of a soluble form of penicillin-binding protein 5 from Escherichia coli and their catalytic properties. J Biol Chem 263 (1988) 2034-2040
    • (1988) J Biol Chem , vol.263 , pp. 2034-2040
    • Nicholas, R.A.1    Strominger, J.L.2
  • 24
    • 0032817244 scopus 로고    scopus 로고
    • Molecular characterization of the SHV-11 β-lactamase of Shigella dysenteriae
    • Ahamed J., and Kundu M. Molecular characterization of the SHV-11 β-lactamase of Shigella dysenteriae. Antimicrob Agents Chemother 43 (1999) 2081-2083
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 2081-2083
    • Ahamed, J.1    Kundu, M.2
  • 25
    • 0031960353 scopus 로고    scopus 로고
    • Interactions of β-lactamases with sanfetrinem (GV 104326) compared to those with imipenem and with oral β-lactams
    • Babini G.S., Yuan M., and Livermore D.M. Interactions of β-lactamases with sanfetrinem (GV 104326) compared to those with imipenem and with oral β-lactams. Antimicrob Agents Chemother 42 (1998) 1168-1175
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1168-1175
    • Babini, G.S.1    Yuan, M.2    Livermore, D.M.3
  • 26
    • 0034663878 scopus 로고    scopus 로고
    • First-derivative spectrophotometric and LC determination of cefuroxime and cefadroxil in urine
    • El-Gindy A., El Walily A.F., and Bedair M.F. First-derivative spectrophotometric and LC determination of cefuroxime and cefadroxil in urine. J Pharm Biomed Anal 23 (2000) 341-352
    • (2000) J Pharm Biomed Anal , vol.23 , pp. 341-352
    • El-Gindy, A.1    El Walily, A.F.2    Bedair, M.F.3
  • 27
    • 33748063296 scopus 로고    scopus 로고
    • A novel ceftazidime-hydrolysing extended-spectrum β-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop
    • Bae I.K., Lee B.H., Hwang H.Y., Jeong S.H., Hong S.G., Chang C.L., et al. A novel ceftazidime-hydrolysing extended-spectrum β-lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop. J Antimicrob Chemother 58 (2006) 315-319
    • (2006) J Antimicrob Chemother , vol.58 , pp. 315-319
    • Bae, I.K.1    Lee, B.H.2    Hwang, H.Y.3    Jeong, S.H.4    Hong, S.G.5    Chang, C.L.6
  • 28
    • 0015327122 scopus 로고
    • Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate
    • O'Callaghan C.H., Morris A., Kirby S.M., and Shingler A.H. Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother 1 (1972) 283-288
    • (1972) Antimicrob Agents Chemother , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.H.4
  • 29
    • 0028125839 scopus 로고
    • Escherichia coli K12 regains its O antigen
    • Liu D., and Reeves P.R. Escherichia coli K12 regains its O antigen. Microbiology 140 (1994) 49-57
    • (1994) Microbiology , vol.140 , pp. 49-57
    • Liu, D.1    Reeves, P.R.2
  • 30
    • 33748505260 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 1b in competitive stationary-phase survival of Escherichia coli
    • Pepper E.D., Farrell M.J., and Finkel S.E. Role of penicillin-binding protein 1b in competitive stationary-phase survival of Escherichia coli. FEMS Microbiol Lett 263 (2006) 61-67
    • (2006) FEMS Microbiol Lett , vol.263 , pp. 61-67
    • Pepper, E.D.1    Farrell, M.J.2    Finkel, S.E.3
  • 31
    • 0018943451 scopus 로고
    • A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking carboxypeptidase 1A
    • Nishimura Y., Suzuki H., Hirota Y., and Park J.T. A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking carboxypeptidase 1A. J Bacteriol 143 (1980) 531-534
    • (1980) J Bacteriol , vol.143 , pp. 531-534
    • Nishimura, Y.1    Suzuki, H.2    Hirota, Y.3    Park, J.T.4
  • 32
    • 0035808477 scopus 로고    scopus 로고
    • Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Ǻ resolution
    • Davies C., White S.W., and Nicholas R.A. Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Ǻ resolution. J Biol Chem 276 (2001) 616-623
    • (2001) J Biol Chem , vol.276 , pp. 616-623
    • Davies, C.1    White, S.W.2    Nicholas, R.A.3
  • 33
    • 0027381457 scopus 로고
    • Penicillin-binding proteins and bacterial resistance to β-lactams
    • Georgopapadakou N.H. Penicillin-binding proteins and bacterial resistance to β-lactams. Antimicrob Agents Chemother 37 (1993) 2045-2053
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2045-2053
    • Georgopapadakou, N.H.1
  • 34
    • 0036033601 scopus 로고    scopus 로고
    • The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli
    • Santos J.M., Lobo M., Matos A.P., De Pedro M.A., and Arraiano C.M. The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli. Mol Microbiol 45 (2002) 1729-1740
    • (2002) Mol Microbiol , vol.45 , pp. 1729-1740
    • Santos, J.M.1    Lobo, M.2    Matos, A.P.3    De Pedro, M.A.4    Arraiano, C.M.5


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