메뉴 건너뛰기




Volumn 157, Issue 9, 2011, Pages 2702-2707

PBP5, PBP6 and DacD play different roles in intrinsic β-lactam resistance of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; AMPICILLIN; ANTIBIOTIC AGENT; BETA LACTAM ANTIBIOTIC; CARBOXYPEPTIDASE; CEFACLOR; CEFADROXIL; CEFALEXIN; CEFALOTIN; CEPHALOSPORIN; CHLORAMPHENICOL; GENOMIC DNA; KANAMYCIN; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; TETRACYCLINE;

EID: 80052356047     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.046227-0     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 0025147735 scopus 로고
    • Testing the susceptibility of bacteria in biofilms to antibacterial agents
    • Anwar, H., Dasgupta, M. K. & Costerton, J. W. (1990). Testing the susceptibility of bacteria in biofilms to antibacterial agents. Antimicrob Agents Chemother 34, 2043-2046.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 2043-2046
    • Anwar, H.1    Dasgupta, M.K.2    Costerton, J.W.3
  • 2
    • 0030463370 scopus 로고    scopus 로고
    • dacD, an Escherichia coli gene encoding a novel penicillinbinding protein (PBP6b) with DD-carboxypeptidase activity
    • Baquero, M. R., Bouzon, M., Quintela, J. C., Ayala, J. A. & Moreno, F. (1996). dacD, an Escherichia coli gene encoding a novel penicillinbinding protein (PBP6b) with DD-carboxypeptidase activity. J Bacteriol 178, 7106-7111.
    • (1996) J Bacteriol , vol.178 , pp. 7106-7111
    • Baquero, M.R.1    Bouzon, M.2    Quintela, J.C.3    Ayala, J.A.4    Moreno, F.5
  • 3
    • 0020313142 scopus 로고
    • Synthesis of penicillinbinding protein 6 by stationary-phase Escherichia coli
    • Buchanan, C. E. & Sowell, M. O. (1982). Synthesis of penicillinbinding protein 6 by stationary-phase Escherichia coli. J Bacteriol 151, 491-494.
    • (1982) J Bacteriol , vol.151 , pp. 491-494
    • Buchanan, C.E.1    Sowell, M.O.2
  • 4
    • 79751527202 scopus 로고    scopus 로고
    • Differences in active-site microarchitecture explain the dissimilar behaviors of PBP5 and 6 in Escherichia coli
    • Chowdhury, C. & Ghosh, A. S. (2011). Differences in active-site microarchitecture explain the dissimilar behaviors of PBP5 and 6 in Escherichia coli. J Mol Graph Model 29, 650-656.
    • (2011) J Mol Graph Model , vol.29 , pp. 650-656
    • Chowdhury, C.1    Ghosh, A.S.2
  • 5
    • 74349093311 scopus 로고    scopus 로고
    • A weak DD-carboxypeptidase activity explains the inability of PBP6 to substitute for PBP5 in maintaining normal cell shape in Escherichia coli
    • Chowdhury, C., Nayak, T. R., Young, K. D. & Ghosh, A. S. (2010). A weak DD-carboxypeptidase activity explains the inability of PBP6 to substitute for PBP5 in maintaining normal cell shape in Escherichia coli. FEMS Microbiol Lett 303, 76-83.
    • (2010) FEMS Microbiol Lett , vol.303 , pp. 76-83
    • Chowdhury, C.1    Nayak, T.R.2    Young, K.D.3    Ghosh, A.S.4
  • 6
    • 0037986022 scopus 로고    scopus 로고
    • CLSI, Seventeenth informational supplement. Document M100-S17. CLSI. Wayne, PA: Clinical and Laboratory Standards Institute
    • CLSI (2007). Performance standards for antimicrobial susceptibility testing. Seventeenth informational supplement. Document M100-S17. CLSI. Wayne, PA: Clinical and Laboratory Standards Institute.
    • (2007) Performance standards for antimicrobial susceptibility testing
  • 7
    • 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. & Young, K. D. (1999). Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J Bacteriol 181, 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
  • 8
    • 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. & Pucci, M. J. (1996). Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli. J Bacteriol 178, 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
  • 9
    • 0027381457 scopus 로고
    • Penicillin-binding proteins and bacterial resistance to b-lactams
    • Georgopapadakou, N. H. (1993). Penicillin-binding proteins and bacterial resistance to b-lactams. Antimicrob Agents Chemother 37, 2045-2053.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2045-2053
    • Georgopapadakou, N.H.1
  • 11
    • 33646701915 scopus 로고    scopus 로고
    • Multiple mutations in or adjacent to the conserved penicillinbinding 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., Mendonça, S., van Vliet, A. H., Pedrazzoli, J., Jr & Kusters, J. G. (2006). Multiple mutations in or adjacent to the conserved penicillinbinding protein motifs of the penicillin-binding protein 1A confer amoxicillin resistance to Helicobacter pylori. Helicobacter 11, 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    Mendonça, S.6    van Vliet, A.H.7    Pedrazzoli Jr., J.8    Kusters, J.G.9
  • 12
    • 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. & Young, K. D. (2003). Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli. J Bacteriol 185, 2178-2186.
    • (2003) J Bacteriol , vol.185 , pp. 2178-2186
    • Ghosh, A.S.1    Young, K.D.2
  • 13
    • 0032581405 scopus 로고    scopus 로고
    • Alterations in high molecular mass penicillin-binding protein 1 associated with b-lactam resistance in Shigella dysenteriae
    • Ghosh, A. S., Kar, A. K. & Kundu, M. (1998). Alterations in high molecular mass penicillin-binding protein 1 associated with b-lactam resistance in Shigella dysenteriae. Biochem Biophys Res Commun 248, 669-672.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 669-672
    • Ghosh, A.S.1    Kar, A.K.2    Kundu, M.3
  • 14
    • 14644387488 scopus 로고    scopus 로고
    • Helical disposition of proteins and lipopolysaccharide in the outer membrane of Escherichia coli
    • Ghosh, A. S. & Young, K. D. (2005). Helical disposition of proteins and lipopolysaccharide in the outer membrane of Escherichia coli. J Bacteriol 187, 1913-1922.
    • (2005) J Bacteriol , vol.187 , pp. 1913-1922
    • Ghosh, A.S.1    Young, K.D.2
  • 15
    • 46249130782 scopus 로고    scopus 로고
    • Physiological functions of D-alanine carboxypeptidases in Escherichia coli
    • Ghosh, A. S., Chowdhury, C. & Nelson, D. E. (2008). Physiological functions of D-alanine carboxypeptidases in Escherichia coli. Trends Microbiol 16, 309-317.
    • (2008) Trends Microbiol , vol.16 , pp. 309-317
    • Ghosh, A.S.1    Chowdhury, C.2    Nelson, D.E.3
  • 16
    • 0026049801 scopus 로고
    • Serine b-lactamases and penicillin-binding proteins
    • Ghuysen, J. M. (1991). Serine b-lactamases and penicillin-binding proteins. Annu Rev Microbiol 45, 37-67.
    • (1991) Annu Rev Microbiol , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 17
    • 0025284661 scopus 로고
    • Resistance of Pseudomonas aeruginosa to cefsulodin: Modification of penicillinbinding protein 3 and mapping of its chromosomal gene
    • Gotoh, N., Nunomura, K. & Nishino, T. (1990). Resistance of Pseudomonas aeruginosa to cefsulodin: modification of penicillinbinding protein 3 and mapping of its chromosomal gene. J Antimicrob Chemother 25, 513-523.
    • (1990) J Antimicrob Chemother , vol.25 , pp. 513-523
    • Gotoh, N.1    Nunomura, K.2    Nishino, T.3
  • 19
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli
    • Höltje, J. V. (1998). Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62, 181-203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 20
    • 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. & De Lorenzo, V. (1995). Site-specific deletions of chromosomally located DNA segments with the multimer resolution system of broad-host-range plasmid RP4. J Bacteriol 177, 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
  • 21
    • 44449131356 scopus 로고    scopus 로고
    • Novel structural analogues of piperine as inhibitors of the NorA efflux pump of Staphylococcus aureus
    • other authors
    • Kumar, A., Khan, I. A., Koul, S., Koul, J. L., Taneja, S. C., Ali, I., Ali, F., Sharma, S., Mirza, Z. M. & other authors (2008). Novel structural analogues of piperine as inhibitors of the NorA efflux pump of Staphylococcus aureus. J Antimicrob Chemother 61, 1270-1276.
    • (2008) J Antimicrob Chemother , vol.61 , pp. 1270-1276
    • Kumar, A.1    Khan, I.A.2    Koul, S.3    Koul, J.L.4    Taneja, S.C.5    Ali, I.6    Ali, F.7    Sharma, S.8    Mirza, Z.M.9
  • 23
    • 63449128597 scopus 로고    scopus 로고
    • b-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein
    • Moya, B., Dötsch, A., Juan, C., Blázquez, J., Zamorano, L., Haussler, S. & Oliver, A. (2009). b-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. PLoS Pathog 5, e1000353.
    • (2009) PLoS Pathog , vol.5
    • Moya, B.1    Dötsch, A.2    Juan, C.3    Blázquez, J.4    Zamorano, L.5    Haussler, S.6    Oliver, A.7
  • 24
    • 0031924072 scopus 로고    scopus 로고
    • Use of recombinant l recombination function to promote gene replacement in Escherichia coli
    • Murphy, K. C. (1998). Use of recombinant l recombination function to promote gene replacement in Escherichia coli. J Bacteriol 180, 2063-2071.
    • (1998) J Bacteriol , vol.180 , pp. 2063-2071
    • Murphy, K.C.1
  • 25
    • 0035026549 scopus 로고    scopus 로고
    • Contributions of PBP5 and DDcarboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli
    • Nelson, D. E. & Young, K. D. (2001). Contributions of PBP5 and DDcarboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli. J Bacteriol 183, 3055-3064.
    • (2001) J Bacteriol , vol.183 , pp. 3055-3064
    • Nelson, D.E.1    Young, K.D.2
  • 26
    • 0036279811 scopus 로고    scopus 로고
    • Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli
    • Nelson, D. E., Ghosh, A. S., Paulson, A. L. & Young, K. D. (2002). Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli. J Bacteriol 184, 3630-3639.
    • (2002) J Bacteriol , vol.184 , pp. 3630-3639
    • Nelson, D.E.1    Ghosh, A.S.2    Paulson, A.L.3    Young, K.D.4
  • 27
    • 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. & Young, K. D. (2004). Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coli. Mol Microbiol 52, 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
  • 28
    • 0018943451 scopus 로고
    • A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase IA
    • Nishimura, Y., Suzuki, H., Hirota, Y. & Park, J. T. (1980). A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase IA. J Bacteriol 143, 531-534.
    • (1980) J Bacteriol , vol.143 , pp. 531-534
    • Nishimura, Y.1    Suzuki, H.2    Hirota, Y.3    Park, J.T.4
  • 29
    • 0002239231 scopus 로고
    • Mode of action of penicillin
    • Park, J. T. & Strominger, J. L. (1957). Mode of action of penicillin. Science 125, 99-101.
    • (1957) Science , vol.125 , pp. 99-101
    • Park, J.T.1    Strominger, J.L.2
  • 30
    • 33748505260 scopus 로고    scopus 로고
    • Role of penicillinbinding protein 1b in competitive stationary-phase survival of Escherichia coli
    • Pepper, E. D., Farrell, M. J. & Finkel, S. E. (2006). Role of penicillinbinding protein 1b in competitive stationary-phase survival of Escherichia coli. FEMS Microbiol Lett 263, 61-67.
    • (2006) FEMS Microbiol Lett , vol.263 , pp. 61-67
    • Pepper, E.D.1    Farrell, M.J.2    Finkel, S.E.3
  • 31
    • 0029841665 scopus 로고    scopus 로고
    • Effect of Oside chain length and composition on the virulence of Shigella flexneri 2a
    • Sandlin, R. C., Goldberg, M. B. & Maurelli, A. T. (1996). Effect of Oside chain length and composition on the virulence of Shigella flexneri 2a. Mol Microbiol 22, 63-73.
    • (1996) Mol Microbiol , vol.22 , pp. 63-73
    • Sandlin, R.C.1    Goldberg, M.B.2    Maurelli, A.T.3
  • 32
    • 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. & Arraiano, C. M. (2002). The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli. Mol Microbiol 45, 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
  • 33
    • 41549090908 scopus 로고    scopus 로고
    • Involvement of O8-antigen in altering b-lactam antibiotic susceptibilities in Escherichia coli
    • Sarkar, S. K. & Ghosh, A. S. (2008). Involvement of O8-antigen in altering b-lactam antibiotic susceptibilities in Escherichia coli. FEMS Microbiol Lett 282, 59-64.
    • (2008) FEMS Microbiol Lett , vol.282 , pp. 59-64
    • Sarkar, S.K.1    Ghosh, A.S.2
  • 34
    • 73549109625 scopus 로고    scopus 로고
    • Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to b-lactam agents
    • Sarkar, S. K., Chowdhury, C. & Ghosh, A. S. (2010). Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to b-lactam agents. Int J Antimicrob Agents 35, 244-249.
    • (2010) Int J Antimicrob Agents , vol.35 , pp. 244-249
    • Sarkar, S.K.1    Chowdhury, C.2    Ghosh, A.S.3
  • 35
    • 0017327167 scopus 로고
    • Properties of the penicillin-binding proteins of Escherichia coli K12
    • Spratt, B. G. (1977). Properties of the penicillin-binding proteins of Escherichia coli K12. Eur J Biochem 72, 341-352.
    • (1977) Eur J Biochem , vol.72 , pp. 341-352
    • Spratt, B.G.1
  • 36
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance
    • Stubbs, K. A., Balcewich, M., Mark, B. L. & Vocadlo, D. J. (2007). Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance. J Biol Chem 282, 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
  • 37
    • 0020972419 scopus 로고
    • Penicillin-binding proteins and the mechanism of action of b-lactam antibiotics
    • Waxman, D. J. & Strominger, J. L. (1983). Penicillin-binding proteins and the mechanism of action of b-lactam antibiotics. Annu Rev Biochem 52, 825-869.
    • (1983) Annu Rev Biochem , vol.52 , pp. 825-869
    • Waxman, D.J.1    Strominger, J.L.2
  • 38
    • 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. & Blaszczak, L. C. (1999). BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins. Antimicrob Agents Chemother 43, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.