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. 1987 Jan;31(1):121–123. doi: 10.1128/aac.31.1.121

Role of porins in intrinsic antibiotic resistance of Pseudomonas cepacia.

T R Parr Jr, R A Moore, L V Moore, R E Hancock
PMCID: PMC174667  PMID: 3032087

Abstract

The measured outer membrane permeability of Pseudomonas cepacia to the beta-lactam nitrocefin was low: approximately 10 times less than that of Escherichia coli and comparable to that of Pseudomonas aeruginosa. The purified P. cepacia porin demonstrated an average single channel conductance in 1 M KCl of 0.23 nS.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benz R., Hancock R. E. Properties of the large ion-permeable pores formed from protein F of Pseudomonas aeruginosa in lipid bilayer membranes. Biochim Biophys Acta. 1981 Aug 20;646(2):298–308. doi: 10.1016/0005-2736(81)90336-9. [DOI] [PubMed] [Google Scholar]
  2. Benz R., Janko K., Boos W., Läuger P. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1978 Aug 17;511(3):305–319. doi: 10.1016/0005-2736(78)90269-9. [DOI] [PubMed] [Google Scholar]
  3. Benz R., Janko K., Läuger P. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1979 Mar 8;551(2):238–247. doi: 10.1016/0005-2736(89)90002-3. [DOI] [PubMed] [Google Scholar]
  4. Benz R., Schmid A., Hancock R. E. Ion selectivity of gram-negative bacterial porins. J Bacteriol. 1985 May;162(2):722–727. doi: 10.1128/jb.162.2.722-727.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fass R. J., Barnishan J. In vitro susceptibilities of nonfermentative gram-negative bacilli other than Pseudomonas aeruginosa to 32 antimicrobial agents. Rev Infect Dis. 1980 Nov-Dec;2(6):841–853. doi: 10.1093/clinids/2.6.841. [DOI] [PubMed] [Google Scholar]
  6. Hancock R. E. Alterations in outer membrane permeability. Annu Rev Microbiol. 1984;38:237–264. doi: 10.1146/annurev.mi.38.100184.001321. [DOI] [PubMed] [Google Scholar]
  7. Hancock R. E., Carey A. M. Outer membrane of Pseudomonas aeruginosa: heat- 2-mercaptoethanol-modifiable proteins. J Bacteriol. 1979 Dec;140(3):902–910. doi: 10.1128/jb.140.3.902-910.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kropp H., Gerckens L., Sundelof J. G., Kahan F. M. Antibacterial activity of imipenem: the first thienamycin antibiotic. Rev Infect Dis. 1985 Jul-Aug;7 (Suppl 3):S389–S410. doi: 10.1093/clinids/7.supplement_3.s389. [DOI] [PubMed] [Google Scholar]
  9. McKevitt A. I., Woods D. E. Characterization of Pseudomonas cepacia isolates from patients with cystic fibrosis. J Clin Microbiol. 1984 Feb;19(2):291–293. doi: 10.1128/jcm.19.2.291-293.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Moore R. A., Hancock R. E. Involvement of outer membrane of Pseudomonas cepacia in aminoglycoside and polymyxin resistance. Antimicrob Agents Chemother. 1986 Dec;30(6):923–926. doi: 10.1128/aac.30.6.923. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Nicas T. I., Hancock R. E. Pseudomonas aeruginosa outer membrane permeability: isolation of a porin protein F-deficient mutant. J Bacteriol. 1983 Jan;153(1):281–285. doi: 10.1128/jb.153.1.281-285.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev. 1985 Mar;49(1):1–32. doi: 10.1128/mr.49.1.1-32.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Russell R. R. Two-dimensional SDS-polyacrylamide gel electrophoresis of heat-modifiable outer-membrane proteins. Can J Microbiol. 1976 Jan;22(1):83–91. doi: 10.1139/m76-011. [DOI] [PubMed] [Google Scholar]
  14. Woodruff W. A., Parr T. R., Jr, Hancock R. E., Hanne L. F., Nicas T. I., Iglewski B. H. Expression in Escherichia coli and function of Pseudomonas aeruginosa outer membrane porin protein F. J Bacteriol. 1986 Aug;167(2):473–479. doi: 10.1128/jb.167.2.473-479.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Zimmermann W., Rosselet A. Function of the outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics. Antimicrob Agents Chemother. 1977 Sep;12(3):368–372. doi: 10.1128/aac.12.3.368. [DOI] [PMC free article] [PubMed] [Google Scholar]

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