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Volumn 1, Issue 2, 1998, Pages 93-98

The role of outer membrane and efflux pumps in the resistance of gram-negative bacteria. Can we improve drug access?

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EID: 0002554841     PISSN: 13687646     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1368-7646(98)80023-X     Document Type: Review
Times cited : (80)

References (45)
  • 1
    • 0027365548 scopus 로고
    • Antibiotic-supersusceptible mutants of Escherichia coli and Salmonella typhimurium
    • Vaara M. Antibiotic-supersusceptible mutants of Escherichia coli and Salmonella typhimurium. Antimicrob Agents Chemother 37 (1993) 2255-2260
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2255-2260
    • Vaara, M.1
  • 2
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido H. Multidrug efflux pumps of gram-negative bacteria. J Bacteriol 178 (1996) 5853-5859
    • (1996) J Bacteriol , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 3
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H., and Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49 (1985) 1-32
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 4
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan S.W., Schirmer T., Rummel G., et al. Crystal structures explain functional properties of two E. coli porins. Nature 358 (1992) 727-733
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3
  • 5
    • 0025968741 scopus 로고
    • Identification and characterization of porins in Pseudomonas aeruginosa
    • Nikaido H., Nikaido K., and Harayama S. Identification and characterization of porins in Pseudomonas aeruginosa. J Biol Chem 266 (1991) 770-779
    • (1991) J Biol Chem , vol.266 , pp. 770-779
    • Nikaido, H.1    Nikaido, K.2    Harayama, S.3
  • 6
    • 0026608845 scopus 로고
    • Outer membranes of gram-negative bacteria are permeable to steroid probes
    • Plésiat P., and Nikaido H. Outer membranes of gram-negative bacteria are permeable to steroid probes. Mol Microbiol 6 (1992) 1323-1333
    • (1992) Mol Microbiol , vol.6 , pp. 1323-1333
    • Plésiat, P.1    Nikaido, H.2
  • 7
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • Nikaido H. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrob Agents Chemother 33 (1989) 1831-1836
    • (1989) Antimicrob Agents Chemother , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 8
    • 0023375673 scopus 로고
    • Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: a quantitative predictive treatment
    • Nikaido H., and Normark S. Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: a quantitative predictive treatment. Mol Microbiol 1 (1987) 29-36
    • (1987) Mol Microbiol , vol.1 , pp. 29-36
    • Nikaido, H.1    Normark, S.2
  • 9
    • 0029845047 scopus 로고    scopus 로고
    • Proton-dependent multidrug efflux systems
    • Paulsen I.T., Brown M.H., and Skurray R.A. Proton-dependent multidrug efflux systems. Microbiol Rev 60 (1996) 575-608
    • (1996) Microbiol Rev , vol.60 , pp. 575-608
    • Paulsen, I.T.1    Brown, M.H.2    Skurray, R.A.3
  • 11
    • 0029129966 scopus 로고
    • Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li X.Z., Nikaido H., and Poole K. Role of MexA-MexB-OprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob Agents Chemother 39 (1995) 1948-1953
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1948-1953
    • Li, X.Z.1    Nikaido, H.2    Poole, K.3
  • 12
    • 0029836682 scopus 로고    scopus 로고
    • Multidrug efflux in intrinsic resistance to trimethoprim and sulfamethoxazole in Pseudomonas aeruginosa
    • Köhler T., Kok M., Michea-Hamzehpour M., et al. Multidrug efflux in intrinsic resistance to trimethoprim and sulfamethoxazole in Pseudomonas aeruginosa. Antimicrob Agents Chemother 40 (1996) 2288-2290
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2288-2290
    • Köhler, T.1    Kok, M.2    Michea-Hamzehpour, M.3
  • 13
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma D., Cook D.N., Alberti M., et al. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol Microbiol 16 (1995) 46-55
    • (1995) Mol Microbiol , vol.16 , pp. 46-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3
  • 14
    • 0000148162 scopus 로고    scopus 로고
    • Regulation of chromosomally mediated multiple antibiotic resistance: the mar regulon
    • Alekshun M.N., and Levy S.B. Regulation of chromosomally mediated multiple antibiotic resistance: the mar regulon. Antimicrob Agents Chemother 41 (1997) 2067-2075
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2067-2075
    • Alekshun, M.N.1    Levy, S.B.2
  • 15
    • 0020057242 scopus 로고    scopus 로고
    • Outer membrane permeability in Pseudomonas aeruginosa: Comparison of a wild-type with an antibiotic-supersusceptible mutant
    • Angus BL, Carey AM, Caron DA, Kropinski AMB, Hancock REW. Outer membrane permeability in Pseudomonas aeruginosa: comparison of a wild-type with an antibiotic-supersusceptible mutant. Antimicrob Agents Chemother 21: 299-309.
    • Antimicrob Agents Chemother , vol.21 , pp. 299-309
    • Angus, B.L.1    Carey, A.M.2    Caron, D.A.3    Kropinski, A.M.B.4    Hancock, R.E.W.5
  • 16
    • 0020441981 scopus 로고
    • Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes
    • Yoshimura F., and Nikaido H. Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes. J Bacteriol 152 (1992) 636-642
    • (1992) J Bacteriol , vol.152 , pp. 636-642
    • Yoshimura, F.1    Nikaido, H.2
  • 17
    • 0031016991 scopus 로고    scopus 로고
    • Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa
    • Köhler T., Michea-Hamzehpour M., Henze U., et al. Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa. Mol Microbiol 23 (1997) 345-354
    • (1997) Mol Microbiol , vol.23 , pp. 345-354
    • Köhler, T.1    Michea-Hamzehpour, M.2    Henze, U.3
  • 19
    • 0027400746 scopus 로고
    • Inhibition of the tetracycline efflux antiport protein by 13-thio-substituted 5-hydroxy-6-deoxytetracyclines
    • Nelson M.L., Park B.H., Andrews J.S., et al. Inhibition of the tetracycline efflux antiport protein by 13-thio-substituted 5-hydroxy-6-deoxytetracyclines. J Med Chem 36 (1993) 370-377
    • (1993) J Med Chem , vol.36 , pp. 370-377
    • Nelson, M.L.1    Park, B.H.2    Andrews, J.S.3
  • 20
    • 0025864903 scopus 로고
    • Efflux-mediated multidrug resistance in Bacillus subtilis: similarities and dissimilarities with the mammalian system
    • Neyfakh A.A., Bidnenko V.E., and Chen L.B. Efflux-mediated multidrug resistance in Bacillus subtilis: similarities and dissimilarities with the mammalian system. Proc Natl Acad Sci USA 88 (1991) 4781-4785
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4781-4785
    • Neyfakh, A.A.1    Bidnenko, V.E.2    Chen, L.B.3
  • 21
    • 77949583985 scopus 로고    scopus 로고
    • Drug-resistant bacteria pose threat to progress in infectious disease reduction
    • Jacob M.I. Drug-resistant bacteria pose threat to progress in infectious disease reduction. Genet Eng News 17 2 (1997) 6
    • (1997) Genet Eng News , vol.17 , Issue.2 , pp. 6
    • Jacob, M.I.1
  • 22
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • Sugawara E., and Nikaido H. OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J Biol Chem 269 (1994) 17981-17987
    • (1994) J Biol Chem , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 23
    • 0022546719 scopus 로고
    • Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F
    • Woodruff W.A., Parr Jr. T.R., and Hancock R. Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F. J Bacteriol 167 (1986) 473-479
    • (1986) J Bacteriol , vol.167 , pp. 473-479
    • Woodruff, W.A.1    Parr Jr., T.R.2    Hancock, R.3
  • 24
    • 0026672679 scopus 로고
    • Reevaluation, using intact cells, of the exclusion limit and role of porin OprF in Pseudomonas aeruginosa outer membrane permeability
    • Bellido F., Martin N.L., Siehnel R.J., and Hancock R. Reevaluation, using intact cells, of the exclusion limit and role of porin OprF in Pseudomonas aeruginosa outer membrane permeability. J Bacteriol 174 (1992) 5196-5203
    • (1992) J Bacteriol , vol.174 , pp. 5196-5203
    • Bellido, F.1    Martin, N.L.2    Siehnel, R.J.3    Hancock, R.4
  • 25
    • 0030778846 scopus 로고    scopus 로고
    • Use of steroids to monitor alterations in the outer membrane of Pseudomonas aeruginosa
    • Plésiat P., Aires J.R., Godard C., and Köhler T. Use of steroids to monitor alterations in the outer membrane of Pseudomonas aeruginosa. J Bacteriol 179 (1997) 7004-7010
    • (1997) J Bacteriol , vol.179 , pp. 7004-7010
    • Plésiat, P.1    Aires, J.R.2    Godard, C.3    Köhler, T.4
  • 26
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara M. Agents that increase the permeability of the outer membrane. Microbiol Rev 56 (1992) 395-411
    • (1992) Microbiol Rev , vol.56 , pp. 395-411
    • Vaara, M.1
  • 27
    • 0020638314 scopus 로고
    • Sensitization of gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide
    • Vaara M., and Vaara T. Sensitization of gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide. Nature 303 (1983) 526-528
    • (1983) Nature , vol.303 , pp. 526-528
    • Vaara, M.1    Vaara, T.2
  • 28
    • 0021257420 scopus 로고
    • Susceptibility of gram-negative bacteria to polymyxin B nonapeptide
    • Vilianen P., and Vaara M. Susceptibility of gram-negative bacteria to polymyxin B nonapeptide. Antimicrob Agents Chemother 25 (1984) 701-705
    • (1984) Antimicrob Agents Chemother , vol.25 , pp. 701-705
    • Vilianen, P.1    Vaara, M.2
  • 29
    • 0031577574 scopus 로고    scopus 로고
    • Antibiotic diffusion pathways in the outer membrane of Pseudomonas aeruginosa
    • Kitahara T., Yoneyama H., and Nakae T. Antibiotic diffusion pathways in the outer membrane of Pseudomonas aeruginosa. Biochem Biophys Res Commun 238 (1997) 457-461
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 457-461
    • Kitahara, T.1    Yoneyama, H.2    Nakae, T.3
  • 32
    • 0021142387 scopus 로고
    • Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes
    • Selsted M.E., Szklarek D., and Lehrer R.I. Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes. Inf Immun 45 (1984) 150-154
    • (1984) Inf Immun , vol.45 , pp. 150-154
    • Selsted, M.E.1    Szklarek, D.2    Lehrer, R.I.3
  • 33
    • 0023683860 scopus 로고
    • Effect of small cationic leukocyte peptides (defensins) on the permeability barrier of the outer membrane
    • Viljanen P., Koski P., and Vaara M. Effect of small cationic leukocyte peptides (defensins) on the permeability barrier of the outer membrane. Inf Immum 56 (1988) 2324-2329
    • (1988) Inf Immum , vol.56 , pp. 2324-2329
    • Viljanen, P.1    Koski, P.2    Vaara, M.3
  • 34
    • 0027474382 scopus 로고
    • Defensins: antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer R.I., Lichtenstein A.K., and Ganz T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu Rev Immunol (1993) 105-128
    • (1993) Annu Rev Immunol , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 35
    • 0025959114 scopus 로고
    • Defensins: endogenous antibiotic peptides of animal cells
    • Lehrer R.I., Ganz T., and Selsted M.E. Defensins: endogenous antibiotic peptides of animal cells. Cell 64 (1991) 229-230
    • (1991) Cell , vol.64 , pp. 229-230
    • Lehrer, R.I.1    Ganz, T.2    Selsted, M.E.3
  • 38
    • 1842373858 scopus 로고    scopus 로고
    • Effects of pH and salinity on the antimicrobial properties of clavanins
    • Lee I.H., Cho Y., and Lehrer R.I. Effects of pH and salinity on the antimicrobial properties of clavanins. Inf Immun 65 (1997) 2898-2903
    • (1997) Inf Immun , vol.65 , pp. 2898-2903
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 39
    • 0029843859 scopus 로고    scopus 로고
    • Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria
    • Vaara M., and Porro M. Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria. Antimicrob Agents Chemother 40 (1996) 1801-1805
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1801-1805
    • Vaara, M.1    Porro, M.2
  • 40
    • 0029824838 scopus 로고    scopus 로고
    • Antiendotoxin activity of cationic peptide antimicrobial agents
    • Gough M., Hancock R., and Kelly N.M. Antiendotoxin activity of cationic peptide antimicrobial agents. Infect Immun 64 (1996) 4922-4927
    • (1996) Infect Immun , vol.64 , pp. 4922-4927
    • Gough, M.1    Hancock, R.2    Kelly, N.M.3
  • 41
    • 0027445909 scopus 로고
    • Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria
    • Piers K., Brown M.H., and Hancock R. Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria. Gene 134 (1993) 7-13
    • (1993) Gene , vol.134 , pp. 7-13
    • Piers, K.1    Brown, M.H.2    Hancock, R.3
  • 42
    • 0024553033 scopus 로고
    • Preferential binding of the neutrophil cytoplasmic granule-derived bactericidal/permeability increasing protein to target bacteria
    • Mannion B.A., Kalatzis E.S., Weiss J., and Elsbach P. Preferential binding of the neutrophil cytoplasmic granule-derived bactericidal/permeability increasing protein to target bacteria. J Immunol 142 (1989) 2807-2812
    • (1989) J Immunol , vol.142 , pp. 2807-2812
    • Mannion, B.A.1    Kalatzis, E.S.2    Weiss, J.3    Elsbach, P.4
  • 43
    • 77949588479 scopus 로고    scopus 로고
    • Evolutionary origins of multidrug and drug-specific efflux pumps in bacteria
    • in press
    • Saier MH Jr, Paulsen IT, Sliwinski MK et al. Evolutionary origins of multidrug and drug-specific efflux pumps in bacteria. FASEB J, in press.
    • FASEB J
    • Saier Jr, M.H.1    Paulsen, I.T.2    Sliwinski, M.K.3
  • 44
    • 0027160409 scopus 로고
    • Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensive alkaloid reserpine
    • Ahmed M., Borsch C.M., Neyfakh A.A., and Schuldiner S. Mutants of the Bacillus subtilis multidrug transporter Bmr with altered sensitivity to the antihypertensive alkaloid reserpine. J Biol Chem 268 (1993) 11086-11089
    • (1993) J Biol Chem , vol.268 , pp. 11086-11089
    • Ahmed, M.1    Borsch, C.M.2    Neyfakh, A.A.3    Schuldiner, S.4
  • 45
    • 0029666248 scopus 로고    scopus 로고
    • Comparative distribution of resistance patterns and serotypes in Pseudomonas aeruginosa isolates from intensive care units and other wards
    • Bert F., and Lambert-Zechovsky N. Comparative distribution of resistance patterns and serotypes in Pseudomonas aeruginosa isolates from intensive care units and other wards. J Antimicrob Chemother 37 (1996) 809-813
    • (1996) J Antimicrob Chemother , vol.37 , pp. 809-813
    • Bert, F.1    Lambert-Zechovsky, N.2


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