OP0595, a new diazabicyclooctane: Mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'

Journal of Antimicrobial Chemotherapy

Volumn 70, Issue 10, 2015, Pages 2779-2786

  Morinaka, Akihiro ^a   Tsutsumi, Yuko ^a   Yamada, Mototsugu ^a   Suzuki, Kenji ^a   Watanabe, Takashi ^a   Abe, Takao ^a   Furuuchi, Takeshi ^a   Inamura, Seiichi ^a   Sakamaki, Yoshiaki ^a   Mitsuhashi, Nakako ^a   Ida, Takashi ^a   Livermore, David M ^b  

^a MEIJI SEIKA KAISHA LTD   (Japan)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AVIBACTAM; AVIBACTAM PLUS CEFTAZIDIME; AZTREONAM; BETA LACTAMASE AMPC; BETA LACTAMASE CTX M; BETA LACTAMASE INHIBITOR; BETA LACTAMASE OXA 1; BETA LACTAMASE OXA 2; BETA LACTAMASE OXA 23; BETA LACTAMASE TEM 1; BETA LACTAMASE TEM 10; CEFEPIME; CEFTAZIDIME; CLAVULANIC ACID; MECILLINAM; MEROPENEM; NITROCEFIN; OP 0595; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; SULBACTAM; TAZOBACTAM; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; AZABICYCLO DERIVATIVE; BETA LACTAM; BETA LACTAMASE; LACTAM; OP0595;

ANTIBACTERIAL ACTIVITY; ANTIBIOTIC SENSITIVITY; ANTIMICROBIAL ACTIVITY; ARTICLE; ENTEROBACTERIACEAE; ENZYME INHIBITION; ESCHERICHIA COLI; IC50; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PHASE CONTRAST MICROSCOPY; STENOTROPHOMONAS MALTOPHILIA; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DRUG EFFECTS; DRUG POTENTIATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; HUMAN; HYDROGEN BOND; METABOLISM; MICROBIAL SENSITIVITY TEST;

ANTI-BACTERIAL AGENTS; AZABICYCLO COMPOUNDS; BETA-LACTAMASE INHIBITORS; BETA-LACTAMASES; BETA-LACTAMS; CATALYTIC DOMAIN; DRUG SYNERGISM; ENZYME ACTIVATION; ESCHERICHIA COLI; HUMANS; HYDROGEN BONDING; INHIBITORY CONCENTRATION 50; LACTAMS; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; MOLECULAR CONFORMATION;

EID: 84943800632     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkv166     Document Type: Article

References (33)

1. Bush K. Proliferation and significance of clinically relevant β-lactamases. Ann N Y Acad Sci 2013; 1277: 84-90.
2. Bush K, Jacoby GA. Updated functional classification of β-lactamases. Antimicrob Agents Chemother 2010; 54: 969-76.
3. Gupta N, Limbago BM, Patel JB et al. Carbapenem-resistant Enterobacteriaceae: epidemiology and prevention. Clin Infect Dis 2011; 53: 60-7.
4. Munoz-Price LS, Poirel L, Bonomo RA et al. Clinical epidemiology of the global expansion of Klebsiella pneumoniae carbapenemases. Lancet Infect Dis 2013; 13: 785-96.
5. Tumbarello M, Viale P, Viscoli C et al. Predictors of mortality in bloodstream infections caused by Klebsiella pneumoniae carbapenemaseproducing K. pneumoniae: importance of combination therapy. Clin Infect Dis 2012; 55: 943-50.
6. Watkins RR, Papp-Wallace KM, Drawz SM et al. Novel β-lactamase inhibitors: a therapeutic hope against the scourge of multidrug resistance. Front Microbiol 2013; 4: 1-8.
7. Zhanel GG, Lawson CD, Adam H et al. Ceftazidime-avibactam: a novel cephalosporin/β-lactamase inhibitor combination. Drugs 2013; 73: 159-77.
8. Livermore DM, Mushtaq S, Warner M et al. Activities of NXL104 combinations with ceftazidime and aztreonam against carbapenemase-producing Enterobacteriaceae. Antimicrob Agents Chemother 2011; 55: 390-4.
9. Hirsch EB, Ledesma KR, Chang KT et al. In vitro activity of MK-7655, a novel β-lactamase inhibitor, in combination with imipenem against carbapenem-resistant Gram-negative bacteria. Antimicrob Agents Chemother 2012; 56: 3753-7.
10. Livermore DM, Warner M, Mushtaq S. Activity of MK-7655 combined with imipenem against Enterobacteriaceae and Pseudomonas aeruginosa. J Antimicrob Chemother 2013; 68: 2286-90.
11. Kano A, Koresawa T, Matsumoto K et al. First in human study to assess safety, tolerability and pharmacokinetics of β-lactamase inhibitor OP0595. In: Abstracts of the Twenty-fifth European Congress of Clinical Microbiology and Infectious Diseases, Copenhagen, 2015. Abstract P0236. ESCMID, Basel, Switzerland.
12. Abe T, Furuuchi T, Sakamaki Y et al. Novel β-Lactamase Inhibitor and Process for Preparing the Same. Meiji Seika Pharma, WO2013180197.
13. Livermore DM, Mushtaq S, Morinaka A et al. Activity of carbapenems with ME1071 (disodium 2,3-diethylmaleate) against Enterobacteriaceae and Acinetobacter spp. with carbapenemases, including NDM enzymes. J Antimicrob Chemother 2013; 68: 153-8.
14. McRee DE. Practical Protein Crystallography. San Diego: Academic Press, 1993.
15. Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Cryst 1997; 30: 1022-5.
16. Emsley P, Lohkamp B, ScottWet al. Features and development of Coot. Acta Cryst 2010; D66: 486-501.
17. Murshudov G, Vagin A, Dodson E. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst 1997; D53: 240-55.
18. Clinical and Laboratory Standards Institute. Performance Standards for Antimicrobial Susceptibility Testing: Twenty-fifth Informational Supplement M100-S25. CLSI, Wayne, PA, USA, 2015.
19. Clinical and Laboratory Standards Institute. Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria That Grow Aerobically- Tenth Edition: Approved Standard M7-A10. CLSI, Wayne, PA, USA, 2015.
20. Iida K, Hirata S, Nakamuta S et al. Inhibition of cell division of Escherichia coli by a new synthetic penicillin, piperacillin. Antimicrob Agents Chemother 1978; 14: 257-66.
21. DalhoffA, Nasu T, Okamoto K. Target affinities of faropenem to and its impact on the morphology of Gram-positive and Gram-negative bacteria. Chemotherapy (Basel) 2003; 49: 172-83.
22. Lahiri SD, Mangani S, Durand-Reville T et al. Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases. Antimicrob Agents Chemother 2013; 57: 2496-505.
23. Lahiri SD, Johnstone MR, Ross PL et al. Avibactam and class C β-lactamases: mechanism of inhibition, conservation of the binding pocket, and implications for resistance. Antimicrob Agents Chemother 2014; 58: 5704-13.
24. Curtis NA, Eisenstadt RL, Turner KA et al. Inhibition of penicillin-binding protein 3 of Escherichia coli K-12. Effects upon growth, viability and outer membrane barrier function. J Antimicrob Chemother 1985; 16: 287-96.
25. Young KD. Why spherical Escherichia coli dies: the inside story. J Bacteriol 2008; 190: 1497-8.
26. Laubacher ME, Ades SE. The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance. J Bacteriol 2008; 190: 2065-74.
27. Verbist L. In-vitro activity of the combinations of ampicillin with mecillinam or with β-lactamase inhibitors against strains resistant to ampicillin. J Antimicrob Chemother 1985; 16: 719-25.
28. Isenberg HD, Sampson-Scherer J, Cleeland R et al. Correlation of the results of antibiotic synergy and susceptibility testing in vitro with results in experimental mouse infections. Crit Rev Microbiol 1982; 10: 1-76.
29. Ehmann DE, Jahic H, Ross PL et al. Kinetics of avibactam inhibition against class A, C, and D β-lactamases. J Biol Chem 2013; 288: 27960-71.
30. Eng RH, Liu R, Smith SM et al. Amdinocillin: interaction with other b-lactam antibiotics for Gram-negative bacteria. Chemotherapy 1988; 34: 18-26.
31. Gutmann L, Vincent S, Billot-Klein D et al. Involvement of penicillinbinding protein 2 with other penicillin-binding proteins in lysis of Escherichia coli by some b-lactam antibiotics alone and in synergistic lytic effect of amdinocillin (mecillinam). Antimicrob Agents Chemother 1986; 30: 906-12.
32. Thulin E, Sundqvist M, Andersson DI. Amdinocillin (mecillinam) resistance mutations in clinical isolates and laboratory-selected mutants of Escherichia coli. Antimicrob Agents Chemother 2015; 59: 1718-27.
33. Joseleau-Petit D, Thévenet D, D'Ari R. ppGpp concentration, growth without PBP2 activity, and growth-rate control in Escherichia coli. Mol Microbiol 1994; 13: 911-7.