Literature DB >> 24235094

A kinetic analysis of the inhibition of FOX-4 β-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic β-lactams and carbapenems.

Krisztina M Papp-Wallace1, Susana Mallo, Christopher R Bethel, Magdalena A Taracila, Andrea M Hujer, Ana Fernández, Julian A Gatta, Kerri M Smith, Yan Xu, Malcolm G P Page, Eric Desarbre, Germán Bou, Robert A Bonomo.   

Abstract

OBJECTIVES: Class C β-lactamases are prevalent among Enterobacteriaceae; however, these enzymes are resistant to inactivation by commercially available β-lactamase inhibitors. In order to find novel scaffolds to inhibit class C β-lactamases, the comparative efficacy of monocyclic β-lactam antibiotics (aztreonam and the siderophore monosulfactam BAL30072), the bridged monobactam β-lactamase inhibitor BAL29880, and carbapenems (imipenem, meropenem, doripenem and ertapenem) were tested in kinetic assays against FOX-4, a plasmid-mediated class C β-lactamase (pmAmpC).
METHODS: The FOX-4 β-lactamase was purified. Steady-state kinetics, electrospray ionization mass spectrometry (ESI-MS) and ultraviolet difference (UVD) spectroscopy were conducted using the β-lactam scaffolds described.
RESULTS: The K(i) values for the monocyclic β-lactams against FOX-4 β-lactamase were 0.04 ± 0.01 μM (aztreonam) and 0.66 ± 0.03 μM (BAL30072), and the Ki value for the bridged monobactam BAL29880 was 8.9 ± 0.5 μM. For carbapenems, the Ki values ranged from 0.27 ± 0.05 μM (ertapenem) to 2.3 ± 0.3 μM (imipenem). ESI-MS demonstrated the formation of stable covalent adducts when the monocyclic β-lactams and carbapenems were reacted with FOX-4 β-lactamase. UVD spectroscopy suggested the appearance of different chromophoric intermediates.
CONCLUSIONS: Monocyclic β-lactam and carbapenem antibiotics are effective mechanism-based inhibitors of FOX-4 β-lactamase, a clinically important pmAmpC, and provide stimulus for the development of new inhibitors to inactivate plasmidic and chromosomal class C β-lactamases.

Entities:  

Keywords:  bridged monobactams; carbapenems; monosulfactam; β-lactamase inhibitors

Mesh:

Substances:

Year:  2013        PMID: 24235094      PMCID: PMC3922156          DOI: 10.1093/jac/dkt434

Source DB:  PubMed          Journal:  J Antimicrob Chemother        ISSN: 0305-7453            Impact factor:   5.790


  48 in total

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2.  Structural basis for imipenem inhibition of class C beta-lactamases.

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4.  Imipenem as substrate and inhibitor of beta-lactamases.

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5.  Occurrence of extended-spectrum and AmpC beta-lactamases in bloodstream isolates of Klebsiella pneumoniae: isolates harbor plasmid-mediated FOX-5 and ACT-1 AmpC beta-lactamases.

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Review 8.  In vitro activity of ertapenem: review of recent studies.

Authors:  Hannah M Wexler
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6.  LN-1-255, a penicillanic acid sulfone able to inhibit the class D carbapenemase OXA-48.

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7.  Analysis of the Structure and Function of FOX-4 Cephamycinase.

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8.  Structure and Characterization of a Covalent Inhibitor of Src Kinase.

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Review 9.  Genetics of Acquired Antibiotic Resistance Genes in Proteus spp.

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  9 in total

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