In vitro antibacterial activity and mechanism of action of J-111,225, a novel 1β-methylcarbapenem, against transferable IMP-1 metallo-β-lactamase producers

Journal of Antimicrobial Chemotherapy

Volumn 45, Issue 3, 2000, Pages 271-276

  Nagano, Rie ^a   Adachi, Yuka ^a   Hashizume, Terutaka ^a   Morishima, Hajime ^a  

^a TAIHO PHARMACEUTICAL CO LTD   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBAPENEM DERIVATIVE; CEFALORIDINE; CEFTAZIDIME; IMIPENEM; MEROPENEM; NITROCEFIN; OFLOXACIN; PIPERACILLIN;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS CEREUS; BACTEROIDES FRAGILIS; ENZYME ACTIVITY; ENZYME INHIBITION; HYDROLYSIS; MINIMUM INHIBITORY CONCENTRATION; PSEUDOMONAS AERUGINOSA; SERRATIA MARCESCENS; STENOTROPHOMONAS MALTOPHILIA;

EID: 0034051621     PISSN: 03057453     EISSN: None     Source Type: Journal    
DOI: 10.1093/jac/45.3.271     Document Type: Article

References (28)

1. Ambler, R. P. (1980). The structure of β-lactamases. Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences 289, 321-31.
2. Rasmussen, B. A. & Bush, K. (1997). Carbapenem-hydrolyzing β-lactamases. Antimicrobial Agents and Chemotherapy 41, 223-32.
3. Watanabe, M., Iyobe, S., Inoue, M. & Mitsuhashi, S. (1991). Transferable imipenem resistance in Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 35, 147-51.
4. IMP among clinically isolated strains of Serratia marcescens. Antimicrobial Agents and Chemotherapy 39, 824-9.
5. IMP) in gram-negative rods resistant to broad-spectrum β-lactams. Journal of Clinical Microbiology 34, 2909-13.
6. IMP. Antimicrobial Agents and Chemotherapy 39, 1612-15.
7. Lee, K., Chong, Y., Shin, H. B. & Yong, D. (1998). Rapid increase of imipenem-hydrolyzing Pseudomonas aeruginosa in a Korean hospital. In Program and Abstracts of the Thirty-Eighth Interscience Conference on Antimicrobial Agents and Chemotherapy, San Diego, CA. Abstract E-85, p. 193. American Society for Microbiology, Washington DC.
8. Cornaglia, G., Riccio, M. L., Mazzariol, A., Lauretti, L., Fontana, R. & Rossolini, G. M. (1999). Appearance of IMP-1 metallo-β-lactamase in Europe. Lancet 353, 899-900.
9. Livermore, D. M. (1997). Acquired carbapenemases. Journal of Antimicrobial Chemotherapy 39, 673-6.
10. Shimizu, A., Sugimoto, Y., Sakuraba, S., Imamura, H., Sato, H., Ohtake, R. et al. (1998). Novel trans-3,5-disubsituted pyrrolidinylthio 1β-methylcarbapenems with potent activity against MRSA and Pseudomonas aeruginosa. In Program and Abstracts of the Thirty-Eighth Interscience Conference on Antimicrobial Agents and Chemotherapy, San Diego, CA. Abstract F-052, p. 246. American Society for Microbiology, Washington DC.
11. Elion, G. B., Singer, S. & Hitchings, H. (1954). Antagonists of nucleic acid derivatives; synergism in combination of biochemically related antimetabolites. Journal of Biological Chemistry 208, 477-88.
12. Saino, Y., Kobayashi, F., Inoue, M. & Mitsuhashi, S. (1982). Purification and properties of inducible penicillin β-lactamase isolated from Pseudomonas maltophilia. Antimicrobial Agents and Chemotherapy 22, 564-70.
13. Payne, D. J., Coleman, K. & Cramp, R. (1991). The automated in-vitro assessment of β-lactamase inhibitors. Journal of Antimicrobial Chemotherapy 28, 775-6.
14. Yang, D., Roll, D. M., Wildey, M. J., Lee, M., Greenstein, W. M., Maiese, W. M. et al. (1994). Inhibition of metallo-β-lactamase by LL-10G568α and LL-10G568β. In Program and Abstracts of the Thirty-Fourth Interscience Conference on Antimicrobial Agents and Chemotherapy, Orlando, FL. Abstract C-056, p. 88. American Society for Microbiology, Washington DC.
15. Bush, K., Freudenberger, J. S. & Sykes, R. B. (1982). Interaction of aztreonam and related monobactams with β-lactamases from gram-negative bacteria. Antimicrobial Agents and Chemotherapy 22, 414-20.
16. Labia, R., Morand, A., Tiwari, K., Sirot, D. & Chanal, C. (1989). Interactions of meropenem with β-lactamases, including enzymes with extended-spectrum activity against third-generation cephalosporins. Journal of Antimicrobial Chemotherapy 24, Suppl. A, 219-23.
17. Sotto, A., Brunschwig, C., O'Callaghan, D., Ramuz, M. & Jourdan, J. (1996). In-vitro evaluation of β-lactamase inhibition by latamoxef and imipenem. Journal of Antimicrobial Chemotherapy 37, 697-701.
18. Carfi, A., Dunee, E., Galleni, M., Frere, J. M. & Dideberg, O. (1997). Metallo-β-lactamase from Bacillus cereus 569h9. Brookhaven Protein Data Bank entry 1BME.
19. Fabiane, S. M., Sohi, M. K., Wan, T., Payne, D. J., Bateson, J. H., Mitchell, T. et al. (1998). Crystal structure of the zinc-dependent β-lactamase from Bacillus cereus at 1.9 Ȧ resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry 37, 12404-11.
20. Concha, N. O., Rasmussen, B. A., Bush, K. & Herzberg, O. (1996). Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4, 823-36.
21. Fitzgerald, P. M., Wu, J. K. & Toney, J. H. (1998). Unanticipated inhibition of the metallo-β-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-Ȧ resolution. Biochemistry 37, 6791-800.
22. Toney, J. H., Fitzgerald, P. M., Grover-Sharma, N., Olson, S. H., May, W. J., Sundelof, J. G. et al. (1998). Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-β-lactamase. Chemistry and Biology 5, 185-96.
23. Ullah, J. H., Walsh, T. R., Taylor, I. A., Emery, D. C., Verma, C. S., Gamblin, S. J., et al. (1998). The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 Ȧ resolution. Journal of Molecular Biology 284, 125-36.
24. Laraki, N., Franceschini, N., Rossolini, G. M., Santucci, P., Meunier, C., de Pauw, E. et al. (1999). Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli. Antimicrobial Agents and Chemotherapy 43, 902-6.
25. Gilpin, M. L., Fulston, M., Payne, D., Cramp, R. & Hood, I. (1995). Isolation and structure determination of two novel phenazines from a Streptomyces with inhibitory activity against metallo-enzymes, including metallo-β-lactamase. Journal of Antibiotics 48, 1081-5.
26. Keynan, S., Hooper, N. M., Felici, A., Amicosante, G. & Turner, A. J. (1995). The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-β-lactamase enzyme CphA. Antimicrobial Agents and Chemotherapy 39, 1629-31.
27. Payne, D. J., Bateson, J. H., Gasson, B. C., Proctor, D., Khushi, T., Farmer, T. H. et al. (1997). Inhibition of metallo-β-lactamases by a series of mercaptoacetic acid thiol ester derivatives. Antimicrobial Agents and Chemotherapy 41, 135-40.
28. Walter, M. W., Felici, A., Galleni, M., Soto, R. P., Adlington, R. M., Baldwin, J. E. et al. (1996). Trifluoromethyl alcohol and ketone inhibitors of metallo-β-lactamases. Bioorganic and Medicinal Chemistry Letters 6, 2455-8.