Prevalence of β-lactamases among 1,072 clinical strains of Proteus mirabilis: A 2-year survey in a French hospital

Antimicrobial Agents and Chemotherapy

Volumn 44, Issue 7, 2000, Pages 1930-1935

  Chanal, C ^a   Bonnet, R ^a   De Champs, C ^a   Sirot, D ^a   Labia, R ^b   Sirot, J ^a  

^a UNIVERSITÉ CLERMONT AUVERGNE   (France)

^b UMR 175   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; BETA LACTAMASE; CEFALOTIN; ISOENZYME; PENICILLINASE; TICARCILLIN; TIMENTIN;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; FRANCE; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PRIORITY JOURNAL; PROMOTER REGION; PROTEUS MIRABILIS; SEQUENCE ANALYSIS; STRAIN DIFFERENCE;

AMOXICILLIN; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; FRANCE; GENE FREQUENCY; HOSPITALS, TEACHING; HUMANS; MICROBIAL SENSITIVITY TESTS; PENICILLIN RESISTANCE; PENICILLINASE; PENICILLINS; PHENOTYPE; PROTEUS MIRABILIS;

EID: 0033945205     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.7.1930-1935.2000     Document Type: Article

References (38)

1. Ambler, R. P., A. F. W. Coulson, J.-M. Frere, J. M. Ghuysen, B. Joris, M. Forsman, R. C. Levesque, G. Tiraby, and S. G. Waley. 1991. A standard numbering scheme for the class A β-lactamases. Biochem. J. 276:269-272.
2. Antibiogram Committee of the French Society for Microbiology. 1998. Statement. Pathol. Biol. 46:1-16.
3. Arlet, G., S. Goussard, P. Courvalin, and A. Philippon. 1999. Sequence of the genes for the TEM-20, TEM-21, TEM-22, and TEM-29 extended-spectrum β-lactamases. Antimicrob. Agents Chemother. 43:969-971.
4. Bauernfeind, A., I. Stemplinger, R. Jungwirth, S. Ernst, and J. M. Casellas. 1996. Sequences of β-lactamase genes encoding CTX-M-1 (MEN-1) and CTX-M-2 and relationship of their amino acid sequences with those of other β-lactamases. Antimicrob. Agents Chemother. 40:509-513.
5. PER-2, which encodes an extended-spectrum class A β-lactamase. Antimicrob. Agents Chemother. 40:616-620.
6. Bobrowski, M. M., M. Matthew, P. T. Barth, N. Datta, N. J. Grinter, A. E. Jacob, P. Kontomichalou, J. W. Dale, and J. T. Smith. 1976. Plasmid-determined beta-lactamase indistinguishable from the chromosomal beta-lactamase of Escherichia coli. J. Bacteriol. 125:149-157.
7. Bonnet, R., C. De Champs, D. Sirot, C. Chanal, R. Labia, and J. Sirot. 1999. Diversity of TEM mutants in Proteus mirabilis. Antimicrob. Agents Chemother. 43:2671-2677.
8. Bret, L., C. Chanal-Claris, D. Sirot, E. B. Chaibi, R. Labia, and J. Sirot. 1998. Chromosomally encoded AmpC-type β-lactamase in a clinical isolate of Proteus mirabilis. Antimicrob. Agents Chemother. 42:1110-1114.
9. Bret, L., C. Chanal, D. Sirot, R. Labia, and J. Sirot. 1996. Characterization of an inhibitor-resistant enzyme IRT-2 derived from TEM-2 β-lactamase produced by Proteus mirabilis strains. J. Antimicrob. Chemother. 38:183-191.
10. TEM genes encoding β-lactamases resistant to clavulanic acid in clinical E. coli. J. Mol. Evol. 44:57-65.
11. Chanal, C., D. Sirot, J. P. Romaszko, L. Bret, and J. Sirot. 1996. Survey of prevalence of extended spectrum β-lactamases among Enterobacteriaceae. J. Antimicrob. Chemother. 38:127-132.
12. Chanal, C. M., D. L. Sirot, A. Petit, R. Labia, A. Morand, J. L. Sirot, and R. A. Cluzel. 1989. Multiplicity of TEM-derived β-lactamases from Klebsiella pneumoniae strains isolated at the same hospital and relationships between the responsible plasmids. Antimicrob. Agents Chemother. 33:1915-1920.
13. Chen, S. T., and R. C. Clowes. 1984. Two improved promoter sequences for the β-lactamase expression arising from a single base-pair substitution. Nucleic Acids Res. 12:3219-3234.
14. De Champs, C., R. Bonnet, D. Sirot, C. Chanal, and J. Sirot. 2000. Clinical relevance of Proteus mirabilis in hospital patients: a two-year survey. J. Antimicrob. Chemother. 45:537-539.
15. Goldstein, F. W., Y. Pean, A. Rosato, J. Gertner, L. Gutmann, and the Vigil'Roc Study Group. 1993. Characterization of ceftriaxone-resistant Enterobacteriaceae: a multicentre study in 26 French hospitals. J. Antimicrob. Chemother. 32:595-603.
16. Goussard, S., and P. Courvalin. 1999. Updated sequence information for TEM β-lactamase genes. Antimicrob. Agents Chemother. 43:367-370.
17. Hawley, D. K., and W. R. McClure. 1983. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 11:2237-2255.
18. Heritage, J., P. M. Hawkey, N. Todd, and I. J. Lewis. 1992 Transposition of the gene encoding a TEM-12 extended-spectrum β-lactamase. Antimicrob. Agents Chemother. 36:1981-1986.
19. Hibbert-Rogers, L. C. F., J. Heritage, N. Todd, and P. M. Hawkey. 1994. Convergent evolution of TEM-26, a β-lactamase with extended spectrum activity. J. Antimicrob. Chemother. 33:707-720.
20. Jarlier, V., T. Fosse, A. Philippon, and the ICU Study Group. 1996. Antibiotic susceptibility in aerobic gram-negative bacilli isolated in intensive care units in 39 French teaching hospitals (ICU study). Intensive Care Med. 22:1057-1065.
21. Labia, R., J. Andrillon, and F. Le Goffic. 1973. Computerized microacidimetric determination of β-lactamase Michaelis-Menten constants. FEBS Lett. 33:42-44.
22. Liu, P. Y. F., D. Gur, L. M. C. Hall, and D. M. Livermore. 1992. Survey of the prevalence of β-lactamases amongst 1000 Gram-negative bacilli isolated consecutively at the Royal London Hospital. J. Antimicrob. Chemother. 30:429-447.
23. Mabilat, C., S. Goussard, W. Sougakoff, R. C. Spencer, and P. Courvalin. 1990. Direct sequencing of the amplified structural gene and promoter for the extended broad-spectrum β-lactamase TEM-9 (RHH-1) of Klebsiella pneumoniae. Plasmid 23:27-34.
24. Mariotte, S., P. Nordmann, and M. H. Nicolas. 1994. Extended-spectrum β-lactamase in Proteus mirabilis. J. Antimicrob. Chemother. 33:925-935.
25. Medeiros, A. A. 1997. Evolution and dissemination of β-lactamases accelerated by generations of β-lactum antibiotics. Clin. Infect. Dis. 24(Suppl. 1):519-545.
26. Nicolas-Chanoine, M. H., H. Chardon, J. L. Avril, Y. Cattoen, J. C. Croix, H. Dabernat, J. Etienne, T. Fosse, J. C. Ghnassia, E. Lecaillon, A. Marmonier, M. Roussel-Delvallez, J. C. Soussy, A. Trevoux, and J. Sirot. 1997. Susceptibility of Enterobacteriaceae to betalactams and fluoroquinolones: a French multicentre study. Clin. Microbiol. Infect. 3(Suppl. 2):74-75.
27. Palzkill, T., K. S. Thomson, C. C. Sanders, E. S. Moland, W. Huang, and T. W. Milligan. 1995. New variant of TEM-10 β-lactamase gene produced by a clinical isolate of Proteus mirabilis. Antimicrob. Agents Chemother. 39: 1199-1200.
28. Philippon, A., G. Arlet, and P. H. Lagrange. 1994. Origin and impact of plasmid-mediated extended-spectrum beta-lactamases. Eur. J. Clin. Microbiol. Infect. Dis. 13(Suppl. 1):17-29.
29. Pitout, J. D. D., K. S. Thomson, N. D. Hanson, A. F. Ehrhardt, E. S. Moland, and C. C. Sanders. 1998. β-Lactamases responsible for resistance to expanded-spectrum cephalosporins in Klebsiella pneumoniae, Escherichia coli, and Proteus mirabilis isolates recovered in South Africa. Antimicrob. Agents Chemother. 42:13511-1354.
30. Russel, D. R., and G. N. Bennet. 1981. Characterization of the β-lactamase promoter of pBR122. Nucleic Acids Res. 11:2517-2532.
31. Sirot, D., J. Sirot, R. Labia, A. Morand, P. Courvalin, A. Darfeuille-Michaud, R. Perroux, and R. Cluzel. 1987. Transferable resistance to third-generation cephalosporins in clinical isolates of Klebsiella pneumoniae: identification of CTX-1, a novel β-lactamase. J. Antimicrob. Chemother. 20: 323-334.
32. Sirot, D. L., F. W. Golstein, C. J. Soussy, A. L. Courtieu, M. O. Husson, J. Lemozy, M. Meyran, C. Morel, R. Ferez, C. Quentin-Noury, M. E. Reverdy, J. M. Scheftel, M. Rosembaum, and Y. Rezvani. 1992. Resistance to cefotaxime and seven other β-lactams in members of the family Enterobacteriaceae: a 3-year survey in France. Antimicrob. Agents Chemother. 36:1677-1681.
33. Sirot, J., C. Chanal, A. Petit, D. Sirot, R. Labia, and G. Gerbaud. 1988. Klebsiella pneumoniae and other Enterobacteriaceae producing novel plasmid-mediated heta-lactamases markedly active against third-generation cephalosporins: epidemiologic studies. Rev. Infect. Dis. 10:850-859.
34. Siu, L. K., P. L. Ho, K. Y. Yuen, S. S. Y. Wong, and P. Y. Chau. 1997. Transferable hyperproduction of TEM-1 β-lactamase in Shigella flexneri due to a point mutation in the Pribnow box. Antimicrob. Agents Chemother. 41:468-470.
35. Sutcliffe, J. G. 1978. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc. Natl. Acad. Sci. USA 75:3737-3741.
36. Verdet, C., G. Ariet, S. Ben Redjeb, A. Ben Hassen, P. H. Lagrange, and A. Philippon. 1998. Characterization of CMY-4, an ampC-type plasmid-mediated β-lactamase in a Tunisian clinical isolate of Proteus mirabilis. FEMS Microbiol. Lett. 169:235-240.
37. Wu, D. Y., L. Ugozzoli, K. B. Pal, and R. B. Wallace. 1989. Allele-specific enzymatic amplification of beta-globin DNA for diagnosis of sickle cell anemia. Proc. Natl. Acad. Sci. USA 86:2757-2760.
38. Wu, P. J., K. Shannon, and I. Phillips. 1995. Mechanisms of hyperproduction of TEM-1 beta-lactamase by clinical isolates of Escherichia coli. J. Antimicrob. Chemother. 36:927-939.