Skip to main content
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1984 Aug;26(2):181–186. doi: 10.1128/aac.26.2.181

Correlation between lipopolysaccharide structure and permeability resistance in beta-lactam-resistant Pseudomonas aeruginosa.

A J Godfrey, L Hatlelid, L E Bryan
PMCID: PMC284115  PMID: 6435513

Abstract

Four beta-lactam-resistant permeability mutants of Pseudomonas aeruginosa PAO503 were studied. The resistance phenotypes were correlated to changes within the lipopolysaccharide. Two of the mutants, PCC1 and PCC19, were shown to differentiate between beta-lactams on the basis of relative hydrophobicity. The more hydrophilic antibiotics were less effective at inhibiting these strains. This phenotype was correlated to the presence of mannose, in measurable quantities, in lipopolysaccharide isolated from these strains. The other two strains, PCC23 and PCC100, differentiated between cephem antibiotics on the basis of electrical charge. The presence of a positive charge markedly increased the relative efficiency of an antibiotic. This correlation did not hold for penam derivatives, with the lower-molecular-weight, dianionic molecules being the most effective. Mutants of this type were changed in the amount of "side chain" sugars or, to minor extent, in their outer membrane protein profiles.

Full text

PDF
181

Images in this article

Selected References

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

  1. Angus B. L., Carey A. M., Caron D. A., Kropinski A. M., Hancock R. E. Outer membrane permeability in Pseudomonas aeruginosa: comparison of a wild-type with an antibiotic-supersusceptible mutant. Antimicrob Agents Chemother. 1982 Feb;21(2):299–309. doi: 10.1128/aac.21.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Biagi G. L., Barbaro A. M., Gamba M. F., Guerra M. C. Partition data of penicillins determined by means of reversed-phase thin-layer chromatography. J Chromatogr. 1969 May 20;41(3):371–379. doi: 10.1016/0021-9673(64)80150-3. [DOI] [PubMed] [Google Scholar]
  3. Godfrey A. J., Bryan L. E. Mutation of Pseudomonas aeruginosa specifying reduced affinity for penicillin G. Antimicrob Agents Chemother. 1982 Feb;21(2):216–223. doi: 10.1128/aac.21.2.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Godfrey A. J., Bryan L. E., Rabin H. R. beta-Lactam-resistant Pseudomonas aeruginosa with modified penicillin-binding proteins emerging during cystic fibrosis treatment. Antimicrob Agents Chemother. 1981 May;19(5):705–711. doi: 10.1128/aac.19.5.705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Haas D., Holloway B. W. R factor variants with enhanced sex factor activity in Pseudomonas aeruginosa. Mol Gen Genet. 1976 Mar 30;144(3):243–251. doi: 10.1007/BF00341722. [DOI] [PubMed] [Google Scholar]
  6. Hancock R. E., Decad G. M., Nikaido H. Identification of the protein producing transmembrane diffusion pores in the outer membrane of Pseudomonas aeruginosa PA01. Biochim Biophys Acta. 1979 Jul 5;554(2):323–331. doi: 10.1016/0005-2736(79)90373-0. [DOI] [PubMed] [Google Scholar]
  7. Hancock R. E., Nikaido H. Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J Bacteriol. 1978 Oct;136(1):381–390. doi: 10.1128/jb.136.1.381-390.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Irvin R. T., Govan J. W., Fyfe J. A., Costerton J. W. Heterogeneity of antibiotic resistance in mucoid isolates of Pseudomonas aeruginosa obtained from cystic fibrosis patients: role of outer membrane proteins. Antimicrob Agents Chemother. 1981 Jun;19(6):1056–1063. doi: 10.1128/aac.19.6.1056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Karkhanis Y. D., Zeltner J. Y., Jackson J. J., Carlo D. J. A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria. Anal Biochem. 1978 Apr;85(2):595–601. doi: 10.1016/0003-2697(78)90260-9. [DOI] [PubMed] [Google Scholar]
  10. Kropinski A. M., Kuzio J., Angus B. L., Hancock R. E. Chemical and chromatographic analysis of lipopolysaccharide from an antibiotic-supersusceptible mutant of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1982 Feb;21(2):310–319. doi: 10.1128/aac.21.2.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kuzio J., Kropinski A. M. O-antigen conversion in Pseudomonas aeruginosa PAO1 by bacteriophage D3. J Bacteriol. 1983 Jul;155(1):203–212. doi: 10.1128/jb.155.1.203-212.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Laemmli U. K., Favre M. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973 Nov 15;80(4):575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  14. Nicas T. I., Hancock R. E. Outer membrane protein H1 of Pseudomonas aeruginosa: involvement in adaptive and mutational resistance to ethylenediaminetetraacetate, polymyxin B, and gentamicin. J Bacteriol. 1980 Aug;143(2):872–878. doi: 10.1128/jb.143.2.872-878.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Nikaido H., Nakae T. The outer membrane of Gram-negative bacteria. Adv Microb Physiol. 1979;20:163–250. doi: 10.1016/s0065-2911(08)60208-8. [DOI] [PubMed] [Google Scholar]
  17. Nikaido H., Rosenberg E. Y. Effect on solute size on diffusion rates through the transmembrane pores of the outer membrane of Escherichia coli. J Gen Physiol. 1981 Feb;77(2):121–135. doi: 10.1085/jgp.77.2.121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Nikaido H., Rosenberg E. Y., Foulds J. Porin channels in Escherichia coli: studies with beta-lactams in intact cells. J Bacteriol. 1983 Jan;153(1):232–240. doi: 10.1128/jb.153.1.232-240.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Perini F., Peters B. P. Fluorometric analysis of amino sugars and derivatized neutral sugars. Anal Biochem. 1982 Jul 1;123(2):357–363. doi: 10.1016/0003-2697(82)90458-4. [DOI] [PubMed] [Google Scholar]
  20. Perini F., Sadow J. B., Hixson C. V. Fluorometric analysis of polyamines, histamine, and 1-methylhistamine. Anal Biochem. 1979 Apr 15;94(2):431–439. doi: 10.1016/0003-2697(79)90386-5. [DOI] [PubMed] [Google Scholar]
  21. Rodríguez-Tebar A., Rojo F., Dámaso D., Vázquez D. Carbenicillin resistance of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1982 Aug;22(2):255–261. doi: 10.1128/aac.22.2.255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Suzuki N. Correlation between pyocin-sensitivity and 2-amino sugar composition of Pseudomonas aeruginosa. FEBS Lett. 1974 Nov 15;48(2):301–305. doi: 10.1016/0014-5793(74)80491-6. [DOI] [PubMed] [Google Scholar]
  23. Sykes R. B. Resistance of Pseudomonas aeruginosa to antimicrobial drugs. Prog Med Chem. 1975;12:333–393. doi: 10.1016/s0079-6468(08)70180-2. [DOI] [PubMed] [Google Scholar]
  24. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  25. Wilkinson S. G., Galbrath L. Studies of lipopolysaccharides from Pseudomonas aeruginosa. Eur J Biochem. 1975 Mar 17;52(2):331–343. doi: 10.1111/j.1432-1033.1975.tb04001.x. [DOI] [PubMed] [Google Scholar]
  26. Wright B. G., Rebers P. A. Procedure for determining heptose and hexose in lipopolysaccharides. Modification of the cysteine-sulfuric acid method. Anal Biochem. 1972 Oct;49(2):307–319. doi: 10.1016/0003-2697(72)90433-2. [DOI] [PubMed] [Google Scholar]
  27. Zimmermann W. Penetration of beta-lactam antibiotics into their target enzymes in Pseudomonas aeruginosa: comparison of a highly sensitive mutant with its parent strain. Antimicrob Agents Chemother. 1980 Jul;18(1):94–100. doi: 10.1128/aac.18.1.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Zimmermann W. Penetration through the gram-negative cell wall: a co-determinant of the efficacy of beta-lactam antibiotics. Int J Clin Pharmacol Biopharm. 1979 Mar;17(3):131–134. [PubMed] [Google Scholar]
  29. 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]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES