The β-lactamase inhibitor avibactam (NnXLl104) does not induce ampC β-lactamase in Enterobacter cloacae

Infection and Drug Resistance

Volumn 6, Issue , 2013, Pages 235-240

  Miossec, Christine ^a   Cclaudon, Monique ^a   Levasseur, Premavathy ^a   Black, Michael T ^a  

^a Novexel   (France)

Author keywords

lactamase; ampC; Avibactam; Induction; NXL104

Indexed keywords

AVIBACTAM; BETA LACTAMASE AMPC; CEFOXITIN; CLAVULANIC ACID; MESSENGER RNA;

ARTICLE; CONTROLLED STUDY; DRUG POTENCY; ENTEROBACTER CLOACAE; GENE INDUCTION; NONHUMAN; PROTEIN EXPRESSION;

EID: 84888999273     PISSN: 11786973     EISSN: None     Source Type: Journal    
DOI: 10.2147/IDR.S53874     Document Type: Article

References (19)

1. Poole K. Resistance to β-lactam antibiotics. Cell Mol Life Sci. 2004;61: 2200-2223.
2. Drawz SM, Bonomo R. Three decades of β-lactamase inhibitors. Clin Microbiol Rev. 2010;23: 160-201.
3. Stachyra T, Péchereau MC, Bruneau JM, et al. Mechanistic studies of the inactivation of TEM-1 and P99 by NXL104, a novel non-β-lactam β-lactamase inhibitor. Antimicrob Agents Chemother. 2010;54: 5132-5138.
4. Ehmann DE, Jahić H, Ross PL, et al. Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor. Proc Natl Acad Sci U S A. 2012;109: 11663-11668.
5. Bonnefoy A, Dupuis-Hamelin C, Steier V, et al. In vitro activity of AVE1330A, an innovative broad-spectrum non-β-lactam β-lactamase inhibitor. J Antimicrob Chemother. 2004;54: 410-417.
6. Livermore DM, Mushtaq S, Warner M, Miossec C, Woodford N. NXL104 combinations versus Enterobacteriaceae with CTX-M extended-spectrum β-lactamases and carbapenemases. J Antimicrob Chemother. 2008;62: 1053-1056.
7. Stachyra T, Levasseur P, Péchereau MC, et al. In vitro activity of the β-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenemases. J Antimicrob Chemother. 2009;64: 326-329.
8. Jones RN. Important and emerging β-lactamase-mediated resistances in hospital-based pathogens: the AmpC enzymes. Diagn Microbiol Infect Dis. 1998;31: 461-466.
9. Jacoby GA. AmpC β-lactamases. Clin Microbiol Rev. 2009;22: 161-182.
10. Kitzis MD, Ferré B, Coutrot A, et al. In vitro activity of combinations of β-lactam antibiotics with β-lactamase inhibitors against cephalosporinase-producing bacteria. Eur J Clin Microbiol Infect Dis. 1989;8: 783-788.
11. Lister PD, Gardner VM, Sanders CC. Clavulanate induces expression of the Pseudomonas aeruginosa AmpC cephalosporinase at physiologically relevant concentrations and antagonizes the antibacterial activity of ticarcillin. Antimicrob Agents Chemother. 1999;43: 882-889.
12. Sanders CC, Sanders WE Jr, Goering RV. In vitro antagonism of β-lactam antibiotics by cefoxitin. Antimicrob Agents Chemother. 1982;21: 968-975.
13. Clinical and Laboratory Standards Institute. Performance Standards for Antimicrobial Susceptibility Testing: Eighteenth International Supplement. Wayne (PA): CLSI; 2010.
14. -ΔΔCT method. Methods. 2001;25: 402-408.
15. Livermore DM, Winstanley TG, Shannon KP. Interpretative reading: recognizing the usual and inferring resistance mechanisms from resistance phenotypes. J Antimicrob Chemother. 2001;48 Suppl 1: 87-102.
16. Dunne WM Jr, Hardin DJ. Use of several inducer and substrate antibiotic combinations in a disk approximation assay format to screen for AmpC induction in patients isolates from Pseudomonas aeruginosa, Enterobacter spp., Citrobacter spp., and Serratia spp. J Clin Microbiol. 2005;43: 5945-5949.
17. Pfaller MA, Jones RN. Antimicrobial susceptibility of inducible AmpC β-lactamase-producing Enterobacteriaceae from the Meropenem Yearly Susceptibility Test Information Collection (MYSTIC) Programme, Europe 1997-2000. Int J Antimicrob Agents. 2002;19: 383-388.
18. Kong KF, Aguila A, Schneper L, Mathee K. Pseudomonas aeruginosa β-lactamase induction requires two permeases, AmpG and AmpP. BMC Microbiol. 2010;10: 328.
19. Mushtaq S, Livermore DM. AmpC induction by ceftaroline. J Antimicrob Chemother. 2010;65: 266-270.