Interactions of OP0595, a novel triple-action diazabicyclooctane, with β-lactams against OP0595-resistant Enterobacteriaceae mutants

Antimicrobial Agents and Chemotherapy

Volumn 60, Issue 1, 2016, Pages 554-560

  Livermore, David M ^a,b   Warner, Marina ^a   Mushtaq, Shazad ^a   Woodford, Neil ^a  

^a PUBLIC HEALTH ENGLAND   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; AVIBACTAM; AZTREONAM; BETA LACTAM DERIVATIVE; CEFEPIME; CEFTAZIDIME; CYCLOOCTANE DERIVATIVE; IMIPENEM; MECILLINAM; MEROPENEM; OP 0595; PIPERACILLIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; AZABICYCLO DERIVATIVE; BETA LACTAMASE; CEPHALOSPORIN DERIVATIVE; DRUG COMBINATION; ESCHERICHIA COLI PROTEIN; ISOPROTEIN; LACTAM; MRDA PROTEIN, E COLI; NACUBACTAM; PENICILLIN BINDING PROTEIN; THIENAMYCIN DERIVATIVE;

ANTIBACTERIAL ACTIVITY; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BACTERIUM ISOLATE; BACTERIUM MUTANT; CONTROLLED STUDY; DRUG POTENTIATION; ENTEROBACTERIACEAE; EXTENDED SPECTRUM BETA LACTAMASE PRODUCING ENTEROBACTERIACEAE; KLEBSIELLA PNEUMONIAE; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL; CHEMISTRY; DRUG COMBINATION; DRUG EFFECTS; GENE EXPRESSION; GENETICS; METABOLISM; MICROBIAL SENSITIVITY TEST; MUTATION; PLASMID;

ANTI-BACTERIAL AGENTS; AZABICYCLO COMPOUNDS; AZTREONAM; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; CEPHALOSPORINS; DRUG COMBINATIONS; DRUG SYNERGISM; ENTEROBACTERIACEAE; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; LACTAMS; MICROBIAL SENSITIVITY TESTS; MUTATION; PENICILLIN-BINDING PROTEINS; PIPERACILLIN; PLASMIDS; PROTEIN ISOFORMS; THIENAMYCINS;

EID: 84957886715     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02184-15     Document Type: Article

References (24)

1. Morinaka A, Tsutsumi Y, Yamada M, Suzuki K, Watanabe T, Abe T, Furuuchi T, Inamura S, Sakamaki Y, Mitsuhashi N, Ida T, Livermore DM. 2015. OP0595, a new diazabicyclooctane: mode of action as a serine β-lactamase inhibitor, antibiotic and β-lactam 'enhancer'. J Antimicrob Chemother 70:2779-2786. http://dx.doi.org/10.1093/jac/dkv166.
2. Livermore DM, Mushtaq S, Warner M, Woodford N. 2015. Activity of OP0595/β-lactam combinations against Gram-negative bacteria with extended-spectrum, AmpC and carbapenem-hydrolysing β-lactamases. J Antimicrob Chemother 70:3032-3041. http://dx.doi.org/10.1093/jac/dkv239.
3. Eng RH, Liu R, Smith SM, Johnson ES, Cherubin CE. 1988. Amdinocillin: interaction with other β-lactam antibiotics for gram-negative bacteria. Chemotherapy (Basel) 34:18-26. http://dx.doi.org/10.1159/000238542.
4. Anderson JD, Eftekhar F. 1983. Study of the enhancement of β-lactam activity by amdinocillin in a model of the human urinary bladder. Am J Med 75:42-47. http://dx.doi.org/10.1016/0002-9343(83)90092-X.
5. Isenberg HD, Sampson-Scherer J, Cleeland R, Titsworth E, Beskid G, Christenson JG, DeLorenzo WF, Unowsky J. 1982. Correlation of the results of antibiotic synergy and susceptibility testing in vitro with results in experimental mouse infections. Crit Rev Microbiol 10:1-76. http://dx.doi.org/10.3109/10408418209113505.
6. Fass RJ. 1980. Activity of mecillinam alone and in combination with other β-lactam antibiotics. Antimicrob Agents Chemother 18:906-912. http://dx.doi.org/10.1128/AAC.18.6.906.
7. Neu JC. 1976. Synergy of mecillinam, a β-amidinopenicillanic acid derivative, combined with β-lactam antibiotics. Antimicrob Agents Chemother 10:535-542. http://dx.doi.org/10.1128/AAC.10.3.535.
8. Kano A, Koresawa T, Matsumoto K, Ouchi S, Kondo K. 2015. First in human study to assess safety, tolerability and pharmacokinetics of beta-lactamase inhibitor OP0595, poster P0236. Twenty-fifth European Congress of Clinical Microbiology and Infectious Diseases, Copenhagen, Denmark, 2015. European Society of Clinical Microbiology and Infectious Diseases, Basel, Switzerland. https://www.escmid.org/escmid-library/online-lecture-library/.
9. Livermore DM, Mushtaq S, Morinaka A, Ida T, Maebashi K, Hope R. 2013. Activity of carbapenems with ME1071 (disodium 2,3-diethylmaleate) against Enterobacteriaceae and Acinetobacter spp. with carbapenemases, including NDM enzymes. J Antimicrob Chemother 68:153-158. http://dx.doi.org/10.1093/jac/dks350.
10. Livermore DM, Warner M, Mushtaq S, Doumith M, Zhang J, Woodford N. 2011. What remains against carbapenem-resistant Enterobacteriaceae? Evaluation of chloramphenicol, ciprofloxacin, colistin, fosfomycin, minocycline, nitrofurantoin, temocillin and tigecycline. Int J Antimicrob Agents 37:415-419. http://dx.doi.org/10.1016/j.ijantimicag.2011.01.012.
11. Clinical and Laboratory Standards Institute. 2015. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, 10th ed. Approved standard M7-A10. Clinical and Laboratory Standards Institute, Wayne, PA.
12. Petit A, Ben-Yaghlane-Bouslama H, Sofer L, Labia R. 1992. Characterization of chromosomally encoded penicillinases in clinical isolates of Klebsiella pneumoniae. J Antimicrob Chemother 29:629-638. http://dx.doi.org/10.1093/jac/29.6.629.
13. Shlaes DM. 2013. New β-lactam-β-lactamase inhibitor combinations in clinical development. Ann N Y Acad Sci 1277:105-114. http://dx.doi.org/10.1111/nyas.12010.
14. Ehmann DE, Jahic H, Ross PL, Gu RF, Hu J, Durand-Réville TF, Lahiri S, Thresher J, Livchak S, Gao N, Palmer T, Walkup GK, Fisher SL. 2013. Kinetics of avibactam inhibition against Class A, C, and D β-lactamases. J Biol Chem 288:27960-27971. http://dx.doi.org/10.1074/jbc.M113.485979.
15. Castanheira M, Mills JC, Costello SE, Jones RN, Sader HS. 2015. Ceftazidime-avibactam activity tested against Enterobacteriaceae isolates from U.S. hospitals (2011 to 2013) and characterization of β-lactamase-producing strains. Antimicrob Agents Chemother 59:3509-3517. http://dx.doi.org/10.1128/AAC.00163-15.
16. Livermore DM, Mushtaq S, Warner M, Zhang J, Maharjan S, Doumith M, Woodford N. 2011. Activities of NXL104 combinations with ceftazidime and aztreonam against carbapenemase-producing Enterobacteriaceae. Antimicrob Agents Chemother 55:390-394. http://dx.doi.org/10.1128/AAC.00756-10.
17. Mushtaq S, Warner M, Williams G, Critchley I, Livermore DM. 2010. Activity of chequerboard combinations of ceftaroline and NXL104 versus β-lactamase-producing Enterobacteriaceae. J Antimicrob Chemother 65:1428-1432. http://dx.doi.org/10.1093/jac/dkq161.
18. Sumita Y, Fukasawa M. 1995. Potent activity of meropenem against Escherichia coli arising from its simultaneous binding to penicillin-binding proteins 2 and 3. J Antimicrob Chemother 36:53-64. http://dx.doi.org/10.1093/jac/36.1.53.
19. Sumita Y, Fukasawa M, Okuda T. 1990. Comparison of two carbapenems, SM-7338 and imipenem: affinities for penicillin-binding proteins and morphological changes. J Antibiot (Tokyo) 43:314-320. http://dx.doi.org/10.7164/antibiotics.43.314.
20. Thulin E, Sundqvist M, Andersson DI. 2015. Amdinocillin (mecillinam) resistance mutations in clinical isolates and laboratory-selected mutants of Escherichia coli. Antimicrob Agents Chemother 59:1718-1727. http://dx.doi.org/10.1128/AAC.04819-14.
21. Doumith M, Mushtaq S, Livermore DM, Woodford N. 2015. Molecular mechanisms of resistance to the new serine-β-lactamase inhibitor OP0595 in Escherichia coli, abstr C-120. Abstr Intersci Conf Antimicrob Agents Chemother (ICAAC)-Int Congr Chemother (ICC), San Diego, CA, 17 to 21 September 2015. American Society for Microbiology, Washington, DC.
22. Joseleau-Petit D, Thévenet D, D'Ari R. 1994. ppGpp concentration, growth without PBP2 activity, and growth rate control in Escherichia coli. Mol Microbiol 13:911-917. http://dx.doi.org/10.1111/j.1365-2958.1994.tb00482.x.
23. Barbour AG, Mayer LW, Spratt BG. 1981. Mecillinam resistance in Escherichia coli: dissociation of growth inhibition and morphologic change. J Infect Dis 143:114-121. http://dx.doi.org/10.1093/infdis/143.1.114.
24. Kahlmeter G, Poulsen HO. 2012. Antimicrobial susceptibility of Escherichia coli from community-acquired urinary tract infections in Europe: the ECO·SENS study revisited. Int J Antimicrob Agents 39:45-51. http://dx.doi.org/10.1016/j.ijantimicag.2011.09.013.