ArticleAntimicrobial agents and chemotherapy2013
IMP-43 and IMP-44 metallo-β-lactamases with increased carbapenemase activities in multidrug-resistant Pseudomonas aeruginosa.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Clinically Significant Carbapenemases in Gram-Negative Pathogens: Molecular Diversity and Advances in β-Lactamase Inhibitor Therapy.Antibiotics (Basel, Switzerland) · 2026Review
- Genetic diversity, biochemical properties, epidemiology, and detection methods of IMP- and VIM-type carbapenemases.Clinical microbiology reviews · 2025Review
- Evaluation of antimicrobial susceptibility tests for Acinetobacter and Pseudomonas species using disks containing a high dose of meropenem.Scientific reports · 2024Article
- Comparative Genomic Analysis of Multi-Drug ResistantMicroorganisms · 2023Article
- Emergence of Carbapenem-resistant Clinical Isolates ofJuntendo Iji zasshi = Juntendo medical journal · 2022Review
- The Antimicrobial Resistance Characteristics of Imipenem-Non-Susceptible, Imipenemase-6-ProducingAntibiotics (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
- Emergence of Carbapenem-Resistant Providencia rettgeri andAntimicrobial agents and chemotherapy · 2020Article
- Suppression of β-Lactam Resistance by Aspergillomarasmine A Is Influenced by both the Metallo-β-Lactamase Target and the Antibiotic Partner.Antimicrobial agents and chemotherapy · 2020Article
- Assessment of a newly developed immunochromatographic assay for NDM-type metallo-β-lactamase producing Gram-negative pathogens in Myanmar.BMC infectious diseases · 2019Article
- Molecular Characterization of Multidrug-ResistantAntimicrobial agents and chemotherapy · 2019Article
- A Modified Carbapenem Inactivation Method, CIMTris, for Carbapenemase Production in Acinetobacter and Pseudomonas Species.Journal of clinical microbiology · 2017Article
- Multidrug-Resistant Sequence Type 235 Pseudomonas aeruginosa Clinical Isolates Producing IMP-26 with Increased Carbapenem-Hydrolyzing Activities in Vietnam.Antimicrobial agents and chemotherapy · 2016Article
- B1-Metallo-β-Lactamases: Where Do We Stand?Current drug targets · 2016Review
- A Carbapenem-Resistant Pseudomonas aeruginosa Isolate Harboring Two Copies of blaIMP-34 Encoding a Metallo-β-Lactamase.PloS one · 2016Article
- Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.Antimicrobial agents and chemotherapy · 2015Article
- First Complete Genome Sequence of Pseudomonas aeruginosa (Schroeter 1872) Migula 1900 (DSM 50071T), Determined Using PacBio Single-Molecule Real-Time Technology.Genome announcements · 2015Article
- Epidemiology and Characteristics of Metallo-β-Lactamase-Producing Pseudomonas aeruginosa.Infection & chemotherapy · 2015Review
- Characterization and distribution of drug resistance associated β-lactamase, membrane porin and efflux pump genes in MDR A. baumannii isolated from Zhenjiang, China.International journal of clinical and experimental medicine · 2015Article
- Dissemination of IMP-6-producing Pseudomonas aeruginosa ST244 in multiple cities in China.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2014Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two novel IMP-type metallo-β-lactamase variants, IMP-43 and IMP-44, were identified in multidrug-resistant Pseudomonas aeruginosa isolates obtained in medical settings in Japan. Analysis of their predicted amino acid sequences revealed that IMP-43 had an amino acid substitution (Val67Phe) compared with IMP-7 and that IMP-44 had two substitutions (Val67Phe and Phe87Ser) compared with IMP-11. The amino acid residue at position 67 is located at the end of a loop close to the active site, consisting of residues 60 to 66 in IMP-1, and the amino acid residue at position 87 forms a hydrophobic patch close to the active site with other amino acids. An Escherichia coli strain expressing blaIMP-43 was more resistant to doripenem and meropenem but not to imipenem than one expressing blaIMP-7. An E. coli strain expressing blaIMP-44 was more resistant to doripenem, imipenem and meropenem than one expressing blaIMP-11. IMP-43 had more efficient catalytic activities against all three carbapenems than IMP-7, indicating that the Val67Phe substitution contributed to increased catalytic activities against carbapenems. IMP-44 had more efficient catalytic activities against all carbapenems tested than IMP-11, as well as increased activities compared with IMP-43, indicating that both the Val67Phe and Phe87Ser substitutions contributed to increased catalytic activities against carbapenems.
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