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Volumn 67, Issue 9, 2012, Pages 2173-2181

A peptide based on homologous sequences of the β-barrel assembly machinery component bamd potentiates antibiotic susceptibility of Pseudomonas aeruginosa

Author keywords

barrel assembly machinery complex; Combination effect; Outer membrane protein

Indexed keywords

AMIKACIN; BETA BARREL ASSEMBLY MACHINERY D PROTEIN; COLISTIN; ERYTHROMYCIN; IMIPENEM; LEVOFLOXACIN; MEROPENEM; OUTER MEMBRANE PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; RIFAMPICIN; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 84865369894     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dks174     Document Type: Article
Times cited : (23)

References (29)
  • 1
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S et al. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol 2006; 61: 151-64.
    • (2006) Mol Microbiol , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3
  • 2
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T, Malinverni J, Ruiz N et al. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 2005; 121: 235-45.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3
  • 3
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: the role of the BAM complex in outer membrane protein assembly
    • Knowles TJ, Scott-Tucker A, Overduin M et al. Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 2009; 7: 206-14.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3
  • 4
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J et al. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 2003; 299: 262-5.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3
  • 5
    • 79952311132 scopus 로고    scopus 로고
    • The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex
    • Noinaj N, Fairman JW, Buchanan SK. The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex. J Mol Biol 2011; 407: 248-60.
    • (2011) J Mol Biol , vol.407 , pp. 248-260
    • Noinaj, N.1    Fairman, J.W.2    Buchanan, S.K.3
  • 6
    • 79956148245 scopus 로고    scopus 로고
    • Crystal structure of BamD: an essential component of the β-barrel assembly machinery of Gram-negative bacteria
    • Sandoval CM, Baker SL, Jansen K et al. Crystal structure of BamD: an essential component of the β-barrel assembly machinery of Gram-negative bacteria. J Mol Biol 2011; 409: 348-57.
    • (2011) J Mol Biol , vol.409 , pp. 348-357
    • Sandoval, C.M.1    Baker, S.L.2    Jansen, K.3
  • 7
    • 35948954841 scopus 로고    scopus 로고
    • First glimpse of the crystal structure of YaeT's POTRA domains
    • Misra R. First glimpse of the crystal structure of YaeT's POTRA domains. ACS Chem Biol 2007; 2: 649-51.
    • (2007) ACS Chem Biol , vol.2 , pp. 649-651
    • Misra, R.1
  • 8
    • 79551577091 scopus 로고    scopus 로고
    • Structure and function of BamE within the outer membrane and the β-barrel assembly machine
    • Knowles TJ, Browning DF, Jeeves M et al. Structure and function of BamE within the outer membrane and the β-barrel assembly machine. EMBO Rep 2011; 12: 123-8.
    • (2011) EMBO Rep , vol.12 , pp. 123-128
    • Knowles, T.J.1    Browning, D.F.2    Jeeves, M.3
  • 9
    • 39749086276 scopus 로고    scopus 로고
    • Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
    • Vuong P, Bennion D, Mantei J et al. Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 2008; 190: 1507-17.
    • (2008) J Bacteriol , vol.190 , pp. 1507-1517
    • Vuong, P.1    Bennion, D.2    Mantei, J.3
  • 10
    • 0038673434 scopus 로고    scopus 로고
    • Surveillance for antimicrobial susceptibility among clinical isolates of Pseudomonas aeruginosa and Acinetobacter baumannii from hospitalized patients in the United States, 1998 to 2001
    • Karlowsky J, Draghi D, Jones M. Surveillance for antimicrobial susceptibility among clinical isolates of Pseudomonas aeruginosa and Acinetobacter baumannii from hospitalized patients in the United States, 1998 to 2001. Antimicrob Agents Chemother 2003; 47: 1681-8.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1681-1688
    • Karlowsky, J.1    Draghi, D.2    Jones, M.3
  • 12
    • 29144471255 scopus 로고    scopus 로고
    • Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Pseudomonas aeruginosa responding to ampicillin, kanamycin, and tetracycline resistance
    • Peng X, Xu C, Ren H et al. Proteomic analysis of the sarcosine-insoluble outer membrane fraction of Pseudomonas aeruginosa responding to ampicillin, kanamycin, and tetracycline resistance. J Proteome Res 2005; 4: 2257-65.
    • (2005) J Proteome Res , vol.4 , pp. 2257-2265
    • Peng, X.1    Xu, C.2    Ren, H.3
  • 13
    • 77950235507 scopus 로고    scopus 로고
    • Beta-tricalcium phosphate exerts osteoconductivity through a2b1 integrin and down-stream MAPK/ERK signaling pathway
    • Lu Z, Zreiqat H. Beta-tricalcium phosphate exerts osteoconductivity through a2b1 integrin and down-stream MAPK/ERK signaling pathway. Biochem Biophys Res Commun 2010; 394: 323-9.
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 323-329
    • Lu, Z.1    Zreiqat, H.2
  • 15
    • 67650672176 scopus 로고    scopus 로고
    • Novel sequential ChIP and simplified basic ChIP protocols for promoter co-occupancy and target gene identification in human embryonic stem cells
    • Medeiros RB, Papenfuss KJ, Hoium B et al. Novel sequential ChIP and simplified basic ChIP protocols for promoter co-occupancy and target gene identification in human embryonic stem cells. BMC Biotechnol 2009; 9: 59.
    • (2009) BMC Biotechnol , vol.9 , pp. 59
    • Medeiros, R.B.1    Papenfuss, K.J.2    Hoium, B.3
  • 16
    • 34248348757 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa: resistance and therapeutic options at the turn of the new millennium
    • Mesaros N, Nordmann P, Plésiat P et al. Pseudomonas aeruginosa: resistance and therapeutic options at the turn of the new millennium. Clin Microbiol Infect 2007; 13: 560-78.
    • (2007) Clin Microbiol Infect , vol.13 , pp. 560-578
    • Mesaros, N.1    Nordmann, P.2    Plésiat, P.3
  • 17
    • 0034117784 scopus 로고    scopus 로고
    • Interplay between the MexA-Mexβ-OprM multidrug efflux system and the outer membrane barrier in the multiple antibiotic resistance of Pseudomonas aeruginosa
    • Li XZ, Zhang L, Poole K. Interplay between the MexA-Mexβ-OprM multidrug efflux system and the outer membrane barrier in the multiple antibiotic resistance of Pseudomonas aeruginosa. J Antimicrob Chemother 2000; 45: 433-6.
    • (2000) J Antimicrob Chemother , vol.45 , pp. 433-436
    • Li, X.Z.1    Zhang, L.2    Poole, K.3
  • 18
    • 0021282341 scopus 로고
    • Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane
    • Hancock RE, Wong PG. Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane. Antimicrob Agents Chemother 1984; 26: 48-52.
    • (1984) Antimicrob Agents Chemother , vol.26 , pp. 48-52
    • Hancock, R.E.1    Wong, P.G.2
  • 19
    • 0035162640 scopus 로고    scopus 로고
    • Identification and characterization of inhibitors of multidrug resistance efflux pumps in Pseudomonas aeruginosa: novel agents for combination therapy
    • Lomovskaya O, Warren MS, Lee A et al. Identification and characterization of inhibitors of multidrug resistance efflux pumps in Pseudomonas aeruginosa: novel agents for combination therapy. Antimicrob Agents Chemother 2001; 45: 105-16.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 105-116
    • Lomovskaya, O.1    Warren, M.S.2    Lee, A.3
  • 20
    • 0035848421 scopus 로고    scopus 로고
    • Addressing the stability of C-capped dipeptide efflux pump inhibitors that potentiate the activity of levofloxacin in Pseudomonas aeruginosa
    • Renau T. Addressing the stability of C-capped dipeptide efflux pump inhibitors that potentiate the activity of levofloxacin in Pseudomonas aeruginosa. Bioorg Med Chem Lett 2001; 11: 663-7.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 663-667
    • Renau, T.1
  • 21
    • 0037060903 scopus 로고    scopus 로고
    • Peptidomimetics of efflux pump inhibitors potentiate the activity of levofloxacin in Pseudomonas aeruginosa
    • Renau TE, Leger R, Yen R et al. Peptidomimetics of efflux pump inhibitors potentiate the activity of levofloxacin in Pseudomonas aeruginosa. Bioorg Med Chem Lett 2002; 12: 763-6.
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 763-766
    • Renau, T.E.1    Leger, R.2    Yen, R.3
  • 22
    • 0032906825 scopus 로고    scopus 로고
    • Resistance to β-lactam antibiotics in Pseudomonas aeruginosa due to interplay between the MexAβ-OprM efflux pump and β-lactamase
    • Nakae T, Nakajima A, Ono T et al. Resistance to β-lactam antibiotics in Pseudomonas aeruginosa due to interplay between the MexAβ-OprM efflux pump and β-lactamase. Antimicrob Agents Chemother 1999; 43: 1301-3.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1301-1303
    • Nakae, T.1    Nakajima, A.2    Ono, T.3
  • 23
    • 77149159117 scopus 로고    scopus 로고
    • Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa
    • Srinivas N, Jetter P, Ueberbacher BJ et al. Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa. Science 2010; 327: 1010-3.
    • (2010) Science , vol.327 , pp. 1010-1013
    • Srinivas, N.1    Jetter, P.2    Ueberbacher, B.J.3
  • 24
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins
    • Sklar JG, Wu T, Gronenberg LS et al. Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Proc Natl Acad Sci USA 2007; 104: 6400-5.
    • (2007) Escherichia coli. Proc Natl Acad Sci USA , vol.104 , pp. 6400-6405
    • Sklar, J.G.1    Wu, T.2    Gronenberg, L.S.3
  • 25
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J. Biogenesis of the Gram-negative bacterial outer membrane. Annu Rev Microbiol 2007; 61: 191-214.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 26
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in Gram-negative bacteria
    • Tokuda H. Biogenesis of outer membranes in Gram-negative bacteria. Biosci Biotechnol Biochem 2009; 73: 465-73.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 27
    • 80052845657 scopus 로고    scopus 로고
    • Antagonistic interactions of Pseudomonas aeruginosa antibiotic resistance mechanisms in planktonic but not biofilm growth
    • Xavier M, Bartolome M, Carlos J et al. Antagonistic interactions of Pseudomonas aeruginosa antibiotic resistance mechanisms in planktonic but not biofilm growth. Antimicrob Agents Chemother 2011; 55: 4560-8.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4560-4568
    • Xavier, M.1    Bartolome, M.2    Carlos, J.3
  • 28
    • 79959468179 scopus 로고    scopus 로고
    • β-Barrel membrane protein assembly by the Bam complex
    • Hagan CL, Silhavy TJ, Kahne D. β-Barrel membrane protein assembly by the Bam complex. Annu Rev Biochem 2011; 80: 189-210.
    • (2011) Annu Rev Biochem , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 29
    • 1342325470 scopus 로고    scopus 로고
    • Differential impact of MexB mutations on substrate selectivity of the OprM multidrug efflux pump of Pseudomonas aeruginosa
    • Middlemiss JK, Poole K. Differential impact of MexB mutations on substrate selectivity of the OprM multidrug efflux pump of Pseudomonas aeruginosa. J Bacteriol 2004; 186: 1258-69.
    • (2004) J Bacteriol , vol.186 , pp. 1258-1269
    • Middlemiss, J.K.1    Poole, K.2


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