ArticleAntimicrobial agents and chemotherapy2013
FIM-1, a new acquired metallo-β-lactamase from a Pseudomonas aeruginosa clinical isolate from Italy.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Global epidemiology of carbapenem-resistantJAC-antimicrobial resistance · 2026Review
- Role of Mobilome in Carbapenem Resistance.Antibiotics (Basel, Switzerland) · 2026Review
- Metallo-β-lactamase-producingFrontiers in microbiology · 2026Review
- Carbapenem-ResistantMicroorganisms · 2025Review
- Evaluation of QuickMIC system for rapid antimicrobial susceptibility testing of Gram-negative pathogens from positive blood cultures, including strains producing extended-spectrum β-lactamases and carbapenemases.Microbiology spectrum · 2025Article
- Identification of a Potential High-Risk Clone and Novel Sequence Type of Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2025Article
- Article
- Novel resistance ICEs carrying theAntimicrobial agents and chemotherapy · 2024Article
- Strategies to Name Metallo-β-Lactamases and Number Their Amino Acid Residues.Antibiotics (Basel, Switzerland) · 2023Review
- The Prevalence of Metallo-Beta-Lactamese-(MβL)-ProducingMicroorganisms · 2023Review
- CRISPR-Based Gene Editing inPharmaceuticals (Basel, Switzerland) · 2023Review
- Antimicrobial Resistance in Romania: Updates on Gram-Negative ESCAPE Pathogens in the Clinical, Veterinary, and Aquatic Sectors.International journal of molecular sciences · 2023Review
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2023Review
- First report of SPM metallo-β-lactamases producingIranian journal of microbiology · 2022Article
- Antibiotic Therapy for Difficult-to-Treat Infections in Lung Transplant Recipients: A Practical Approach.Antibiotics (Basel, Switzerland) · 2022Review
- An IncP-2 plasmid sublineage associated with dissemination ofEmerging microbes & infections · 2021Article
- Characterization ofAntibiotics (Basel, Switzerland) · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Diversity and Distribution of Resistance Markers inMicroorganisms · 2021Review
- Mobile Carbapenemase Genes inFrontiers in microbiology · 2021Review
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Acquired metallo-β-lactamases (MBLs) are resistance determinants of increasing clinical importance in Gram-negative bacterial pathogens, which confer a broad-spectrum β-lactam resistance, including carbapenems. Several such enzymes have been described since the 1990s. In the present study, a novel acquired MBL, named FIM-1, was identified and characterized. The bla(FIM-1) gene was cloned from a multidrug-resistant Pseudomonas aeruginosa clinical isolate (FI-14/157) cultured from a patient with a vascular graft infection in Florence, Italy. The isolate belonged in the sequence type 235 epidemic clonal lineage. The FIM-1 enzyme is a member of subclass B1 and, among acquired MBLs, exhibited the highest similarity (ca. 40% amino acid identity) with NDM-type enzymes. In P. aeruginosa FI-14/157, the bla(FIM-1) gene was apparently inserted into the chromosome and associated with ISCR19-like elements that were likely involved in the capture and mobilization of this MBL gene. Transfer experiments of the bla(FIM-1) gene to an Escherichia coli strain or another P. aeruginosa strain by conjugation or electrotransformation were not successful. The FIM-1 protein was produced in E. coli and purified by two chromatography steps. Analysis of the kinetic parameters, carried out with the purified enzyme, revealed that FIM-1 has a broad substrate specificity, with a preference for penicillins (except the 6α-methoxy derivative temocillin) and carbapenems. Aztreonam was not hydrolyzed. Detection of this novel type of acquired MBL in a P. aeruginosa clinical isolate underscores the increasing diversity of such enzymes that can be encountered in the clinical setting.
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