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. 1983 Jan;23(1):91–97. doi: 10.1128/aac.23.1.91

Characterization of beta-lactamase induction in Enterobacter cloacae.

T D Gootz, C C Sanders
PMCID: PMC184623  PMID: 6402977

Abstract

The induction of beta-lactamase was studied in a strain of Enterobacter cloacae. A wide variety of beta-lactam compounds were found to induce beta-lactamase in this organism, and the degree of induction was directly related to the stability of the inducer to degradation by the enzyme. The kinetics of the induction process were consistent with a system normally under repressor control, suggesting a direct interaction of the beta-lactam compound with a repressor protein in the E. cloacae cells. Although these characteristics are common to many inducible systems in gram-negative organisms, the induction of beta-lactamase in this strain was not subject to catabolite repression with glucose and remained unaffected by exogenous cyclic AMP in the culture medium. This suggests that the organization and function of the beta-lactamase regulatory genes in E. cloacae are unlike those of other inducible gene systems, such as those composing the well-characterized lactose operon in Escherichia coli.

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Selected References

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

  1. Gootz T. D., Sanders C. C., Sanders W. E., Jr In vitro activity of furazlocillin (Bay k 4999) compared with those of mezlocillin, piperacillin, and standard beta-lactam antibiotics. Antimicrob Agents Chemother. 1979 Jun;15(6):783–791. doi: 10.1128/aac.15.6.783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Grimm H. Bacteriological antagonism between acylureidopenicillins and cephalosporins. J Antimicrob Chemother. 1982 Jan;9 (Suppl A):31–34. doi: 10.1093/jac/9.suppl_a.31. [DOI] [PubMed] [Google Scholar]
  3. Harwood J., Smith D. H. Catabolite repression of chloramphenicol acetyl transferase synthesis in E. coli K12. Biochem Biophys Res Commun. 1971 Jan 8;42(1):57–62. doi: 10.1016/0006-291x(71)90361-5. [DOI] [PubMed] [Google Scholar]
  4. Hennessey T. D. Inducible beta-lactamase in Enterobacter. J Gen Microbiol. 1967 Nov;49(2):277–285. doi: 10.1099/00221287-49-2-277. [DOI] [PubMed] [Google Scholar]
  5. Jaurin B., Grundström T., Edlund T., Normark S. The E. coli beta-lactamase attenuator mediates growth rate-dependent regulation. Nature. 1981 Mar 19;290(5803):221–225. doi: 10.1038/290221a0. [DOI] [PubMed] [Google Scholar]
  6. Kuck N. A., Testa R. T., Forbes M. In vitro and in vivo antibacterial effects of combinations of beta-lactam antibiotics. Antimicrob Agents Chemother. 1981 Apr;19(4):634–638. doi: 10.1128/aac.19.4.634. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LEIVE L. A NONSPECIFIC INCREASE IN PERMEABILITY IN ESCHERICHIA COLI PRODUCED BY EDTA. Proc Natl Acad Sci U S A. 1965 Apr;53:745–750. doi: 10.1073/pnas.53.4.745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Lampe M. F., Allan B. J., Minshew B. H., Sherris J. C. Mutational enzymatic resistance of Enterobacter species to beta-lactam antibiotics. Antimicrob Agents Chemother. 1982 Apr;21(4):655–660. doi: 10.1128/aac.21.4.655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. MAKMAN R. S., SUTHERLAND E. W. ADENOSINE 3',5'-PHOSPHATE IN ESCHERICHIA COLI. J Biol Chem. 1965 Mar;240:1309–1314. [PubMed] [Google Scholar]
  11. Minami S., Yotsuji A., Inoue M., Mitsuhashi S. Induction of beta-lactamase by various beta-lactam antibiotics in Enterobacter cloacae. Antimicrob Agents Chemother. 1980 Sep;18(3):382–385. doi: 10.1128/aac.18.3.382. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Neu H. C., Labthavikul P. Comparative in vitro activity of N-formimidoyl thienamycin against gram-positive and gram-negative aerobic and anaerobic species and its beta-lactamase stability. Antimicrob Agents Chemother. 1982 Jan;21(1):180–187. doi: 10.1128/aac.21.1.180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Nordström K., Sykes R. B. Induction kinetics of beta-lactamase biosynthesis in Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1974 Dec;6(6):734–740. doi: 10.1128/aac.6.6.734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Preheim L. C., Penn R. G., Sanders C. C., Goering R. V., Giger D. K. Emergence of resistance to beta-lactam and aminoglycoside antibiotics during moxalactam therapy of Pseudomonas aeruginosa infections. Antimicrob Agents Chemother. 1982 Dec;22(6):1037–1041. doi: 10.1128/aac.22.6.1037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rosselet A., Zimmermann W. Mutants of Pseudomonas aeruginosa with impaired -lactamase inducibility and increased sensitivity to -lactam antibiotics. J Gen Microbiol. 1973 Jun;76(2):455–457. doi: 10.1099/00221287-76-2-455. [DOI] [PubMed] [Google Scholar]
  16. Sanders C. C., Moellering R. C., Jr, Martin R. R., Perkins R. L., Strike D. G., Gootz T. D., Sanders W. E., Jr Resistance to cefamandole: a collaborative study of emerging clinical problems. J Infect Dis. 1982 Jan;145(1):118–125. doi: 10.1093/infdis/145.1.118. [DOI] [PubMed] [Google Scholar]
  17. Sanders C. C., Sanders W. E., Jr Emergence of resistance to cefamandole: possible role of cefoxitin-inducible beta-lactamases. Antimicrob Agents Chemother. 1979 Jun;15(6):792–797. doi: 10.1128/aac.15.6.792. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sanders C. C., Sanders W. E., Jr, Goering R. V. In vitro antagonism of beta-lactam antibiotics by cefoxitin. Antimicrob Agents Chemother. 1982 Jun;21(6):968–975. doi: 10.1128/aac.21.6.968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sanders C. C., Sanders W. E., Jr Sch 29482: comparative activity against Enterobacteriaceae multiply-resistant to beta-lactam antibiotics and mycobacteria. J Antimicrob Chemother. 1982 Feb;9 (Suppl 100):59–69. doi: 10.1093/jac/9.suppl_c.59. [DOI] [PubMed] [Google Scholar]
  20. Sykes R. B., Matthew M. The beta-lactamases of gram-negative bacteria and their role in resistance to beta-lactam antibiotics. J Antimicrob Chemother. 1976 Jun;2(2):115–157. doi: 10.1093/jac/2.2.115. [DOI] [PubMed] [Google Scholar]
  21. Then R. L., Angehrn P. Trapping of nonhydrolyzable cephalosporins by cephalosporinases in Enterobacter cloacae and Pseudomonas aeruginosa as a possible resistance mechanism. Antimicrob Agents Chemother. 1982 May;21(5):711–717. doi: 10.1128/aac.21.5.711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Van Tiel-Menkvled G. J., Rezee A., De Graaf F. K. Production and excretion of cloacin DF13 by Escherichia coli harboring plasmid CloDF13. J Bacteriol. 1979 Nov;140(2):415–423. doi: 10.1128/jb.140.2.415-423.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wanner B. L., Kodaira R., Neidhardt F. C. Regulation of lac operon expression: reappraisal of the theory of catabolite repression. J Bacteriol. 1978 Dec;136(3):947–954. doi: 10.1128/jb.136.3.947-954.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Waterworth P. M., Emmerson A. M. Dissociated resistance among cephalosporins. Antimicrob Agents Chemother. 1979 Apr;15(4):497–503. doi: 10.1128/aac.15.4.497. [DOI] [PMC free article] [PubMed] [Google Scholar]

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