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Evidence for nonspecific induction of beta-lactamase in overproducing variants ofEnterobacter cloacae andCitrobacter freundii

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Abstract

Induction of chromosomally mediatedβ-lactamases was studied in clinical isolates ofEnterobacter cloacae andCitrobacter freundii. Whereas isolates resistant to ampicillin and cefoxitin exhibited an inducible enzyme, those sensitive to both agents did not. Cefoxitin and above all imipenem proved the most efficacious enzyme inducers. Variants among these inducible isolates which produced large amounts ofβ-lactamase could be selected in the presence of cefamandole. In each of these selected variants constitutive enzyme production was markedly enhanced by induction, even with compounds lacking induction potency for the corresponding wild strains. Moreover, these variants could also be induced non-specifically, i.e. by non-β-lactam compounds. Production of large amounts of enzyme was associated with resistance to all availableβ-lactam compounds.

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References

  1. Sanders, C. C.: Novel resistance selected by the new expanded-spectrum cephalosporins: a concern. Journal of Infectious Diseases 1983, 147: 585–589.

    PubMed  Google Scholar 

  2. Seeberg, A. H., Tolxdorff-Neutzling, R. M., Wiedemann, B.: Chromosomalβ-lactamase ofEnterobacter cloacae are responsible for resistance to third-generation cephalosporins. Antimicrobial Agents and Chemotherapy 1983, 23: 918–925.

    PubMed  Google Scholar 

  3. Gootz, Th. D., Sanders, C. C., Goering, R. V.: Resistance to cefamandole: derepression of beta-lactamase by cefoxitin and mutation inEnterobacter cloacae. Journal of Infectious Diseases 1982, 146: 34–42.

    PubMed  Google Scholar 

  4. Cullmann, W., Opferkuch, W., Stieglitz, M., Dick, W.: Influence of spontaneous and inducibleβ-lactamase production on the antimicrobial activity of recently developedβ-lactam compounds. Chemotherapy 1984, 30: 175–181.

    PubMed  Google Scholar 

  5. Cullmann, W., Dick, W., Dalhoff, A.: Nonspecific induction ofβ-lactamase inEnterobacter cloacae. Journal of General Microbiology 1984, 130: 1781–1786.

    PubMed  Google Scholar 

  6. Knippers, R.: Molekulare Genetik. Georg Thieme Verlag, Stuttgart, 1982.

    Google Scholar 

  7. Cullmann, W., Flensberg, Th., Opferkuch, W., Stieglitz, M., Wiedemann, B.: Correlation ofβ-lactamase production and resistance toβ-lactam antibiotics inEnterobacteriaceae. Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene (A) 1982, 252: 480–489.

    Google Scholar 

  8. Gootz, Th. D., Sanders, C. C.: Characterization ofβ- lactamase induction inEnterobacter cloacae. Antimicrobial Agents and Chemotherapy 1983, 23: 91–97.

    PubMed  Google Scholar 

  9. Markwell, M. A. K., Hass, S. M., Bieber, L. L., Tolbert, N. K.: A modification of the L.owry procedure to simplify protein determinations in membrane and lipoprotein samples. Analytical Biochemistry 1978, 87: 206–210.

    PubMed  Google Scholar 

  10. Jones, R. V., Wilson, H. W., Novick jr., W. J., Barry, A. L., Thomberry, C.: In-vitro evaluation of CentaR, a new beta-lactamase susceptible chromogenic cephalosporin reagent. Journal of Clinical Microbiology 1982, 15: 954–958.

    PubMed  Google Scholar 

  11. Minami, S., Yotsuji, A., Inoue, M., Mitsuhashi, S.: Induction ofβ-lactamase by variousβ-lactam antibiotics inEnterobacter cloacae. Antimicrobial Agents and Chemotherapy 1980, 18: 382–385.

    PubMed  Google Scholar 

  12. Dalhoff, A., Cullmann, W.: Evidence for non-specific induction ofβ-lactamases inPseudomonas aeruginosa. Journal of Antimicrobial Chemotherapy 1984, 14: 349–359.

    PubMed  Google Scholar 

  13. Then, R. L.: Properties of Ro 13-9904 as a substrate and inhibitor ofβ-lactamases. Chemotherapy 1981, 27, Supplement: 25–31.

    PubMed  Google Scholar 

  14. Sykes, R. B.: The classification and terminology of enzymes that hydrolyzeβ-lactam antibiotics. Journal of Infectious Diseases 1982, 145: 762–765.

    PubMed  Google Scholar 

  15. Cullmann, W., Dick, W.: Investigations ofβ-lactamase stability of recently developedβ-lactam compounds: study of enzyme kinetics. Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene (A) 1983, 253: 426–434.

    Google Scholar 

  16. Normark, St., Edlund, Th., Grundström, Th., Bergström, S., Wolf-Watz, H.:Escherichia coli K-12 mutants hyperproducing chromosomalβ-lactamase by gene repetitions. Journal of Bacteriology 1977, 132: 912–922.

    PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Medical Microbiology and Immunology, Ruhr-University Bochum, PO Box 102148, 4630, Bochum 1, FRG

    W. Cullmann

  2. Department of Clinical Chemistry, Lukas Hospital, 4004, Neuss, FRG

    W. Dick

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  1. W. Cullmann
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  2. W. Dick
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Cullmann, W., Dick, W. Evidence for nonspecific induction of beta-lactamase in overproducing variants ofEnterobacter cloacae andCitrobacter freundii . Eur. J, Clin. Microbiol. 4, 34–40 (1985). https://doi.org/10.1007/BF02148657

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