Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France

Antimicrobial Agents and Chemotherapy

Volumn 44, Issue 4, 2000, Pages 891-897

  Poirel, Laurent ^a   Naas, Thierry ^a   Nicolas, Delphine ^a   Collet, Louis ^b   Bellais, Samuel ^a   Cavallo, Jean Didier ^c   Nordmann, Patrice ^a  

^a BICÊTRE HOSPITAL   (France)

^b INSTITUT PAOLI CALMETTES   (France)

^c Hop d'Instruction des Armees Begin   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMOXICILLIN; AZTREONAM; BACTERIAL ENZYME; BETA LACTAMASE; CARBAPENEM DERIVATIVE; CEFALOTIN; CEFEPIME; CEFOPERAZONE; CEFOTAXIME; CEFOXITIN; CEFPIROME; CEFSULODIN; CEFTAZIDIME; CEFUROXIME; CEPHALOSPORIN DERIVATIVE; CEPHAMYCIN DERIVATIVE; DRUG METABOLIZING ENZYME; EDETIC ACID; IMIPENEM; LATAMOXEF; MEROPENEM; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; TICARCILLIN; UREIDOPENICILLIN DERIVATIVE; ZINC;

AMINO ACID SEQUENCE; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL GENE; BACTERIUM ISOLATE; DNA SEQUENCE; DRUG HYDROLYSIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; FRANCE; GENE CASSETTE; GENE EXPRESSION; INTEGRON; ISOELECTRIC POINT; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; BETA-LACTAMASES; CARBAPENEMS; CLONING, MOLECULAR; DNA, BACTERIAL; FRANCE; GENES, BACTERIAL; KINETICS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PLASMIDS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS INFECTIONS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION;

EID: 0034023159     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.4.891-897.2000     Document Type: Article

References (28)

1. IMP. Antimicrob. Agents Chemother. 39: 1612-1615.
2. Bellais, S., S. Léotard, L. Poirel, T. Naas, and P. Nordmann. 1999. Molecular characterization of a carbapenem-hydrolyzing β-lactamase from Chryseobacterium (Flavobacterium) indologenes. FEMS Microbiol. Lett. 171:127-132.
3. Bush, K. 1998. Metallo-enzymes: a class apart. Clin. Infect. Dis. 27(Suppl. 1): S48-S53.
4. Collis, C. M., and R. M. Hall. 1995. Expression of antibiotic resistance genes in the integrated cassettes of integrons. Antimicrob. Agents Chemother. 39: 155-162.
5. Da Silva, G. J., R. Leitão, and L. Peixe. 1999. Emergence of carbapenem-hydrolyzing enzymes in Acinetobacter baumannii clinical isolates. J. Clin. Microbiol. 37:2109-2110.
6. Felici, A., G. Amicosante, A. Oratore, R. Strom, P. Ledent, B. Joris, L. Fanuel, and J.-M. Frère. 1993. An overview of the kinetic parameters of class B β-lactamases. Biochem. J. 291:151-155.
7. IMP. Antimicrob. Agents Chemother. 42:2006-2011.
8. Hussain, M., A. Carlino, M. J. Madonna, and J. O. Lampen. 1985 Cloning and sequencing of the metallothioprotein β-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol. 164:223-229.
9. IMP-containing Pseudomonax aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes. Antimicrob. Agents Chemother. 43:890-901.
10. VIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrob. Agents Chemother. 43:1584-1590.
11. Lévesque, C., S. Brassard, J. Lapointe, and P. H. Roy. 1994. Diversity and relative strength of tandem promoters for the antibiotic-resistance genes of several integrons. Gene 142:49-54.
12. Massidda, O., G. M. Rossolini, and G. Satta. 1991. The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-β-lactamases. J. Bacteriol. 173:4611-4617.
13. Matsumura, N., S. Minami, Y. Watanabe, S. Iyobe, and S. Mitsuhashi. 1999. Role of permeability in the activities of β-lactams against gram-negative bacteria which produce a group 3 β-lactamase. Antimicrob. Agents Chemother. 43:2084-2086.
14. Nielsen, H., J. Engelbrecht, S. Brunak, and G. Von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
15. Osano, E., Y. Arakawa, R. Wacharotayankun, M. Ohta, T. Horii, H. Ito, F. Yoshimura, and N. Kato, 1994. Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38:71-78.
16. Poirel, L., M. Guibert, D. Girlich, T. Naas, and P. Nordmann. 1999. Cloning, sequence analyses, expression and distribution of ampC-ampR from Morganella morganii clinical isolates. Antimicrob. Agents Chemother. 43:769-776.
17. Poirel, L., T. Naas, M. Guibert, E. B. Chaibi, R. Labia, and P. Nordmann. 1999. Molecular and biochemical characterization of VEB-1, a novel class A extended-spectrum β-lactamase encoded by an Escherichia coli integron gene. Antimicrob. Agents Chemother. 43:573-581.
18. Rasmussen, B. A., and K. Bush. 1997. Carbapenem-hydrolyzing β-lactamases. Antimicrob. Agents Chemother. 41:223-232.
19. Rasmussen, B. A., Y. Gluzman, and F. P. Tally. 1990. Cloning and sequencing of the class B β-lactamase gene (ccrA) from Bacteroides fragilis TAL3636. Antimicrob. Agents Chemother. 34:1590-1592.
20. Recchia, G. D., and R. M. Hall. 1995. Gene cassettes: a new class of mobile elements. Microbiology 141:3015-3027.
21. Rossolini, G. M., N. Franceschini, M. L. Riccio, P. S. Mercuri, M. Perilli, M. Galleni, J.-M. Frère, and G. Amicosante. 1998. Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B β-lactamase showing a broad substrate profile. Biochem. J. 332:145-152.
22. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
23. Stokes, H. W., D. B. O'Gorman, G. D. Recchia, M. Parsekhian, and R. M. Hall. 1997. Structure and function of 59-base element recombination sites associated with mobile gene cassettes. Mol. Microbiol. 26:731-745.
24. Ullah, J. H., T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Vermas, S. J. Gamblin, and J. Spencer. 1998. The crystal structure of the L-1 metallo-β-lactamase from Stenotrophomonas maltophilia at 12.7 A resolution. J. Mol. Biol. 284:125-136.
25. Walsh, T. R., L. Hall, S. J. Assinder, W. W. Nichols, S. J. Cartwright, A. P. MacGowan, and P. M. Bennett. 1994. Sequence analysis of the L-1 metallo β-lactamase from Xanthomonas maltophilia. Biochim. Biophys. Acta 1218: 199-201.
26. Walther-Rasmussen, J., A. H. Johnsen, and N. Hoiby. 1998. Terminal truncations in AmpC β-lactamase from a clinical isolate of Pseudomonas aeruginosa. Eur. J. Biochem. 263:478-485.
27. Wang, Z., W. Fast, and S. J. Benkovic. 1999. On the mechanism of the metallo-β-lactamase from Bacteroides fragilis. Biochemistry 38:10013-10023.
28. West, S. E. H., and B. H. Iglewski. 1998. Codon usage in Pseudomonas aeroginosa. Nucleic Acids Res. 16:9323-9335.