1887

Abstract

Surmmary

Back mutations from the TRC-1 -lactamase to the TEM-1 enzyme were selected . The revertant -lactamase was obtained from strain J62.2 carrying plasmid pUK901 which encodes the TRC-1 -lactamase. The revertant was obtained after repeated subculture of J62.2 (pUK901) in amoxycillin 512 mg/L for 5 days. The revertant -lactamase had the same pI as TEM-1 (5.4) and had restored inhibition by clavulanic acid (ID50 reduced from 4.2 to 0.15 ). The prevalence of these -lactamases in the clinical population may be the result of a two-way flux, with mutations in both forward and backward directions.

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1995-06-01
2023-02-01
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References

  1. Medeiros A. A. β-Lactamases. Br Med Bull 1984; 40:18–27
    [Google Scholar]
  2. Sanders C. C., Sanders W. E. Beta-lactam resistance in Gram negative bacteria—global trends and clinical impact. Clin Infect Dis 1992; 15:824–839
    [Google Scholar]
  3. Thomson C. J., Amyes S. G. B. Prospects for expanding the use of β-lactamase inhibitors. J Med Microbiol 1992; 37:297–298
    [Google Scholar]
  4. Rolinson G. N. Evolution of β-lactamase inhibitors. Rev Infect Dis 1991; 13: Suppl 9S727–S732
    [Google Scholar]
  5. Thomson C. J., Amyes S. G. B. Molecular epidemiology of the plasmid-encoded TEM-1 β-lactamase in Scotland. Epidemiol Infect 1993; 110:117–125
    [Google Scholar]
  6. Shanahan P. M. A., Thomson C. J., Amyes S. G. B. β-Lactam resistance in aerobic commensal faecal flora. Int J Chemother 1994; 3:259–266
    [Google Scholar]
  7. Philippon A., Labia R., Jacoby G. Extended-spectrum β-lactamases. Antimicrob Agents Chemother 1989; 33:1131–1136
    [Google Scholar]
  8. Payne D. J., Cramp R. Determination of ID50 values for 35 plasmid mediated β-lactamases. Abstracts of the First International Congress on the Management of Infection 1992; 10B7:65
    [Google Scholar]
  9. Thomson C. J., Amyes S. G. B. TRC-1: emergence of a clavulanic acid-resistant TEM β-lactamase in clinical strain. FEMS Microbiol Lett 1992; 91:113–118
    [Google Scholar]
  10. Vedel G., Belaaouaj A., Gilly L. Clinical isolates of Escherichia coli producing TRI β-lactamases: novel TEM-enzymes conferring resistance to β-lactamase inhibitors. J Antimicrob Chemother 1992; 30:449–462
    [Google Scholar]
  11. Thomson C. J., Amyes S. G. B. Selection of variants of the TEM-1 β-lactamase, encoded by a plasmid of clinical origin, with increased resistance to β-lactamase inhibitors. J Antimicrob Chemother 1993; 31:655–664
    [Google Scholar]
  12. Davis B. D., Mingioli E. S. Mutants of Escherichia coli requiring methionine or vitamin B12. J Bacteriol 1950; 60:17–28
    [Google Scholar]
  13. Takahashi S., Nagano Y. Rapid procedure for isolation of plasmid DNA and application to epidemiological analysis. J Clin Microbiol 1984; 20:608–613
    [Google Scholar]
  14. Matthew M., Harris A. M., Marshall M. J., Ross G. W. The use of analytical isoelectric focusing for detection and identification of β-lactamases. J Gen Microbiol 1975; 88:169–178
    [Google Scholar]
  15. Reid A. J., Amyes S. G. B. Plasmid penicillin resistance in Vibrio cholerae: identification of new β-lactamase SAR-1. Antimicrob Agents Chemother 1986; 30:245–247
    [Google Scholar]
  16. French G., Ling J. Amoxycillin/clavulanate resistant Escherichia coli . Lancet 1988; 1:704
    [Google Scholar]
  17. Sanders C. C., Iaconis J. P., Bodey G. D., Samonis G. Resistance to ticarcillin-potassium clavulanate among clinical isolates of the family Enterobacteriaceae: role of PSE-1 β-lactamase and high levels of TEM-1 and SHV-1 and problems with false susceptibility in disk diffusion tests. Antimicrob Agents Chemother 1988; 32:1365–1369
    [Google Scholar]
  18. Seetulsingh P. S., Hall L. M. C., Livermore D. M. Activity of clavulanate combinations against TEM-1 β-lactamase producing Escherichia coli isolates obtained in 1982 and 1989. J Antimicrob Chemother 1991; 27:749–759
    [Google Scholar]
  19. Wu P. J., Shannon K., Phillips I. β-Lactamases and susceptibility to β-lactam antibiotics in Escherichia coli . J Antimicrob Chemother 1992; 30:868–871
    [Google Scholar]
  20. Delaire M., Labia R., Samama J.-P., Masson J.-M. Site directed mutagenesis at the active site of Escherichia coli TEM-1 β-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J Biol Chem 1992; 267:20600–20606
    [Google Scholar]
  21. Manavathu E. K., Lerner S. A., Fekete T., Perlin M. H., Ziaja E., Price S. Characterization of mutant TEM β-lactamase that confers resistance to ampicillin (amp) plus clavulanic acid (CA). Abstracts of the 30th Interscience Congress on Antimicrobial Agents and Chemotherapy 1990 No. 281 133
    [Google Scholar]
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