ArticleAntimicrobial agents and chemotherapy2010
Efficacy of calcium-EDTA as an inhibitor for metallo-β-lactamase in a mouse model of Pseudomonas aeruginosa pneumonia.
Article in Antimicrobial agents and chemotherapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 67 citations in OpenAlex.
- Chelate-conjugated β-lactams resensitize metallo-β-lactamase IMP-1-producing gram-negative bacteria against carbapenem antibiotics.Microbiology spectrum · 2026Article
- Rapid Detection of Carbapenemase-Producing Enterobacterales Using a Luminescent Whole-Cell Biosensor.ACS infectious diseases · 2026Article
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- Cloning, Expression, and Characterization of GDSL-Type Lipolytic Enzyme Genes fromJournal of microbiology and biotechnology · 2025Article
- Development andRSC advances · 2025Article
- Unseen Enemy: Mechanisms of Multidrug Antimicrobial Resistance in Gram-Negative ESKAPE Pathogens.Antibiotics (Basel, Switzerland) · 2025Review
- Elucidation of critical chemical moieties of metallo-β-lactamase inhibitors and prioritisation of target metallo-β-lactamases.Journal of enzyme inhibition and medicinal chemistry · 2024Review
- Restoring colistin sensitivity in colistin-resistantmSphere · 2024Article
- Ca-EDTA restores the activity of ceftazidime-avibactam or aztreonam against carbapenemase-producingiScience · 2023Article
- Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface.Current opinion in chemical biology · 2022Review
- Drug development concerning metallo-β-lactamases in gram-negative bacteria.Frontiers in microbiology · 2022Review
- EDTA and Taurolidine Affect Pseudomonas aeruginosa VirulenceMicrobiology spectrum · 2021Article
- Novel colistin-EDTA combination for successful eradication of colistin-resistant Klebsiella pneumoniae catheter-related biofilm infections.Scientific reports · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Metallo-β-Lactamases: Structure, Function, Epidemiology, Treatment Options, and the Development Pipeline.Antimicrobial agents and chemotherapy · 2020Review
- Antibiotic Resistance Profiles, Molecular Mechanisms and Innovative Treatment Strategies ofMicroorganisms · 2020Review
- Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism.Biomolecules · 2020Review
- Article
- SAR Studies Leading to the Identification of a Novel Series of Metallo-β-lactamase Inhibitors for the Treatment of Carbapenem-Resistant Enterobacteriaceae Infections That Display Efficacy in an Animal Infection Model.ACS infectious diseases · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we have evaluated the efficacy of calcium-EDTA (Ca-EDTA) as an inhibitor of bacterial metalloenzymes, such as metallo-β-lactamase (MBL) and other proteases, in a mouse model of Pseudomonas aeruginosa pneumonia. The simultaneous presence of Ca-EDTA (32 μg/ml) reduced the MICs of imipenem (IPM) in all MBL-producing P. aeruginosa isolates (IMP-1, -2, -7, and -10 and VIM-2) but not non-MBL-producing strains. In the pneumonia model, mice were intranasally infected with MBL-producing P. aeruginosa and then kept under conditions of hyperoxia to mimic ventilator-associated pneumonia. With both intranasal and subcutaneous administrations, Ca-EDTA significantly potentiated survival benefits of IPM compared to those of IPM alone. Ca-EDTA combination therapy induced a significant reduction of the bacterial burden in the lungs (P < 0.05). Furthermore, the inhibition activity of Ca-EDTA against MBL activity was confirmed by using the purified IMP-1 enzyme, which was characterized by a 50% inhibitory concentration (IC(50)) of 55 ± 8.2 μM. Finally, the protective effects of Ca-EDTA were demonstrated by culture supernatant-induced epithelial cell damage and acute lung injury in mice. These data suggest the therapeutic potential of Ca-EDTA not only by the blocking of MBLs but also by neutralizing tissue-damaging metalloproteases in P. aeruginosa infections.
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