Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa

Antimicrobial Agents and Chemotherapy

Volumn 47, Issue 2, 2003, Pages 582-587

  Murphy, Tanya A ^a   Simm, Alan M ^a   Toleman, Mark A ^a   Jones, Ronald N ^b   Walsh, Timothy R ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b JMI LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; AMPICILLIN; AZLOCILLIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBAPENEM DERIVATIVE; CARBENICILLIN; CEFALORIDINE; CEFALOTIN; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEFUROXIME; CEPHALOSPORIN DERIVATIVE; CLAVULANIC ACID; DIPICOLINIC ACID; EDETIC ACID; IMIPENEM; LATAMOXEF; MEROPENEM; NITROCEFIN; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; PROTEIN SPM 1; TAZOBACTAM; TICARCILLIN; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME KINETICS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PSEUDOMONAS AERUGINOSA;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; BETA-LACTAMS; PSEUDOMONAS AERUGINOSA;

EID: 0037310952     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.47.2.582-587.2003     Document Type: Article

References (50)

1. IMP. Antimicrob. Agents Chemother. 39:1612-1615.
2. Avison, M. B., C. S. Higgins, C. J. von Heldreich, P. M. Bennett, and T. R. Walsh. 2001. Plasmid location and molecular heterogeneity of the L1 and L2 β-lactamase genes of Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 45:413-419.
3. Bellais, S., S. Leotard, 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.
4. Bellais, S., L. Poirel, S. Leotard, T. Naas, and P. Nordmann. 2000. Genetic diversity of carbapenem-hydrolysing metallo-β-lactamases from Chryseobacterium (Flavobacterium) indologenes. Antimicrob. Agents Chemother. 44: 3028-3034.
5. Bennett, P. M. 1999. Integrons and gene cassettes: a genetic construction kit for bacteria. J. Antimicrob. Chemother. 43:1-4.
6. Boschi, L., P. S. Mercuri, M. L. Riccio, G. Amicosante, M. Galleni, J. M. Frere, and G. M. Rossolini. 2000. The Legionella (Fluoribacter) gormanii metallo-β-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 β-lactamases. Antimicrob. Agents Chemother. 44:1538-1543.
7. Carfi, A., S. Pares, E. Duee, M. Galleni, C. Duez, J. M. Frere, and O. Dideberg. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14:4914-4921.
8. Chu, Y. W., M. Afzal-Shah, E. T. Houang, M. I. Palepou, D. J. Lyon, N. Woodford, and D. M. Livermore. 2001. IMP-4, a novel metallo-β-lactamase from nosocomial Acinetobacter spp. collected in Hong Kong between 1994 and 1998. Antimicrob. Agents Chemother. 45:710-714.
9. Concha, N. O., C. A. Janson, P. Rowling, S. Pearson, C. A. Cheever, B. P. Clarke, C. Lewis, M. Galleni, J. M. Frere, D. J. Payne, J. H. Bateson, and S. S. Abdel-Meguid. 2000. Crystal structure of the IMP-1 metallo-β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39:4288-4298.
10. Concha, N. O., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
11. Cornaglia, G., M. L. Riccio, A. Mazzariol, L. Lauretti, R. Fontana, and G. M. Rossolini. 1999. Appearance of IMP-1 metallo-β-lactamase in Europe. Lancet 353:899-900.
12. Franceschini, N., B. Caravelli, J. D. Docquier, M. Galleni, J. M. Frere, G. Amicosante, and G. M. Rossolini. 2000. Purification and biochemical characterization of the VIM-1 metallo-β-lactamase. Antimicrob. Agents Chemother. 44:3003-3007.
13. Galleni, M., N. Franceschini, B. Quinting, L. Fattorini, G. Orefici, A. Oratore, J. M. Frere, and G. Amicosante. 1994. Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum D316 to study potentially poor substrates and inhibitory β-lactam compounds. Antimicrob. Agents Chemother. 38:1608-1614.
14. Galleni, M., J. Lamotte-Brasseur, G. M. Rossolini, J. Spencer, O. Dideberg, and J. M. Frere. 2001. Standard numbering scheme for class B β-lactamases. Antimicrob. Agents Chemother. 45:660-663.
15. IMP-7. Antimicrob. Agents Chemother. 46:255-258.
16. Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
17. Hawkey, P. M., J. Xiong, H. Ye, H. Li, and F. H. M'Zali. 2001. Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid in Citrobacter youngae from the People's Republic of China. FEMS Microbiol. Lett. 194:53-57.
18. Hernandez Valladares, M., A. Felici, G. Weber, H. W. Adolph, M. Zeppezauer, G. M. Rossolini, G. Amicosante, J. M. Frere, and M. Galleni. 1997. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-β-lactamase activity and stability. Biochemistry 36:11534-11541.
19. IMP among clinically isolated strains of Serratia marcescens. Antimicrob. Agents Chemother. 39:824-829.
20. Koh, T. H., G. S. Babini, N. Woodford, L. H. Sng, L. M. Hall, and D. M. Livermore. 1999. Carbapenem hydrolysing IMP-1 β-lactamase in Klebsiella pneumoniae from Singapore. Lancet 353:2162.
21. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
22. Laraki, N., N. Franceschini, G. M. Rossolini, P. Santucci, C. Meunier, E. de Pauw, G. Amicosante, J. M. Frere, and M. Galleni. 1999. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrob. Agents Chemother. 43: 902-906.
23. IMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes. Antimicrob. Agents Chemother. 43:890-901.
24. VIM, a new integron-borne metallo-β-lactamase gene from a Pseudomonas aeruginosa clinical isolate. Antimicrob. Agents Chemother. 43:1584-1590.
25. Livermore, D. M., and N. Woodford. 2000. Carbapenemases: a problem in waiting? Curr. Opin. Microbiol. 3:489-495.
26. Massidda, O., G. M. Rossolini, and G. Satta. 1991. The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-β-lac tamases. J. Bacteriol. 173:4611-4617.
27. Mavroidi, A., A. Tsakris, E. Tzelepi, S. Pournaras, V. Loukova, and L. S. Tzouvelekis. 2000. Carbapenem-hydrolysing VIM-2 metallo-β-lactamase in Pseudomonas aeruginosa from Greece. J. Antimicrob. Chemother. 46:1041-1042.
28. Mercuri, P. S., F. Bouillenne, L. Boschi, J. Lamotte-Brasseur, G. Amicosante, B. Devreese, J. van Beeumen, J. M. Frere, G. M. Rossolini, and M. Galleni. 2001. Biochemical characterization of the FEZ-1 metallo-β-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli. Antimicrob. Agents Chemother. 45:1254-1262.
29. Poirel, L., T. Naas, D. Nicolas, L. Collet, S. Bellais, J. D. Cavallo, and P. Nordmann. 2000. 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. Antimicrob. Agents Chemother. 44:891-897.
30. Prats, G., E. Miro, B. Mirelis, L. Poirel, S. Bellais, and P. Nordmann. 2002. First isolation of a carbapenem-hydrolysing β-lactamase in Pseudomonas aeruginosa in Spain. Antimicrob. Agents Chemother. 46:932-933.
31. 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.
32. IMP allelic variants carried by gene cassettes of different phylogeny. Antimicrob. Agents Chemother. 44:1229-1235.
33. Rossolini, G. M., M. A. Condemi, F. Pantanella, J. D. Docquier, G. Amicosante, and M. C. Thaller. 2001. Metallo-β-lactamase producers in environmental microbiota: new molecular class B enzyme in Janthinobacterium lividum. Antimicrob. Agents Chemother. 45:837-844.
34. Rossolini, G. M., N. Franceschini, M. L. Riccio, P. S. Mercuri, M. Perilli, M. Galleni, J. M. Frere, 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.
35. Sanschagrin, F., J. Dufresne, and R. C. Levesque. 1998. Molecular heterogeneity of the L1 metallo-β-lactamase family from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 42:1245-1248.
36. Scott, W. R. P., P. H. Hunenberger, I. G. Tironi, A. E. Mark, S. R. Bileter, J. Fennen, A. E. Torda, T. Huber, and P. Kruger. 1999. The GROMOS biomolecular simulation package. J. Phys. Chem. 103:3596-3607.
37. Seigel, I. H. 1975. Enzyme kinetics behaviour and analysis of rapid equilibrium and steady-state enzyme systems. John Wiley & Sons, Inc., New York, N.Y.
38. Senda, K., Y. Arakawa, K. Nakashima, H. Ito, S. Ichiyama, K. Shimokata, N. Kato, and M. Ohta. 1996. Multifocal outbreaks of metallo-β-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems. Antimicrob. Agents Chemother. 40:349-353.
39. Simm, A. M., C. S. Higgins, S. T. Pullan, M. B. Avison, P. Niumsup, O. Erdozain, P. M. Bennett, and T. R. Walsh. 2001. A novel metallo-β-lactamase, Mb11b, produced by the environmental bacterium Caulobacter crescentus. FEBS Lett. 509:350-354.
40. Srinivasan, N., K. Guruprasad, and T. L. Blundell. 1996. Comparative modelling of proteins, vol. 170, Oxford University Press Inc., New York, N.Y.
41. Thomson, J. S., and M. H. Malamy 1990. Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus β-lactamase II. J. Bacteriol. 172:2584-2593.
42. Toleman, M., A. M. Simm, T. A. Murphy, A. C. Gales, D. J. Biedenbach, R. N. Jones, and T. R. Walsh. Molecular characterization of SPM-1, a novel metallo-β-lactamase isolated in Latin America: report from the SENTRY antimicrobial programme. J. Antimicrob. Chemother. 50:673-679.
43. Tysall, L., M. W. Stockdale, P. R. Chadwick, M. F. Palepou, K. J. Towner, D. M. Livermore, and N. Woodford. 2002. IMP-1 carbapenemase detected in an Acinetobacter clinical isolate from the UK. J. Antimicrob. Chemother. 49:217-218.
44. Ullah, J. H., T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Verma, S. J. Gamblin, and J. Spencer. 1998. The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Å resolution. J. Mol. Biol. 284:125-136.
45. Walsh, T. R., W. A. Neville, M. H. Haran, D. Tolson, D. J. Payne, J. H. Bateson, A. P. MacGowan, and P. M. Bennett. 1998. Nucleotide and amino acid sequences of the metallo-β-lactamase, ImiS, from Aeromonas veronii bv. sobria. Antimicrob. Agents Chemother. 42:436-439.
46. Winston, R. L., and M. C. Fitzgerald. 1998. Concentration and desalting of protein samples for mass spectrometry analysis. Anal. Biochem. 262:83-85.
47. Woodford, N., M. F. Palepou, G. S. Babini, B. Holmes, and D. M. Livermore. 2000. Carbapenemases of Chryseobacterium (Flavobacterium) meningosepticum: distribution of blaB and characterization of a novel metallo-β-lactamase gene, blaB3, in the type strain, NCTC 10016. Antimicrob. Agents Chemother. 44:1448-1452.
48. Yan, J. J., P. R. Hsueh, W. C. Ko, K. T. Luh, S. H. Tsai, H. M. Wu, and J. J. Wu. 2001. Metallo-β-lactamases in clinical Pseudomonas isolates in Taiwan and identification of VIM-3, a novel variant of the VIM-2 enzyme. Antimicrob. Agents Chemother. 45:2224-2228.
49. Yan, J. J., W. C. Ko, and J. J. Wu. 2001. Identification of a plasmid encoding SHV-12, TEM-1, and a variant of IMP-2 metallo-β-lactamase, IMP-8, from a clinical isolate of Klebsiella pneumoniae. Antimicrob. Agents Chemother. 45:2368-2371.
50. Yano, H., A. Kuga, R. Okamoto, H. Kitasato, T. Kobayashi, and M. Inoue. 2001. Plasmid-encoded metallo-β-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem. Antimicrob. Agents Chemother. 45:1343-1348.