Antimicrobial agents and chemotherapy, 2015-11, Vol.59 (11), p.7090-7093
2015
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Details
- Autor(en) / Beteiligte
- Titel
- IMP-51, a novel IMP-type metallo-β-lactamase with increased doripenem- and meropenem-hydrolyzing activities, in a carbapenem-resistant Pseudomonas aeruginosa clinical isolate
- Ist Teil von
- Antimicrobial agents and chemotherapy, 2015-11, Vol.59 (11), p.7090-7093
- Ort / Verlag
- United States: American Society for Microbiology
- Erscheinungsjahr
- 2015
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- A meropenem-resistant Pseudomonas aeruginosa isolate was obtained from a patient in a medical setting in Hanoi, Vietnam. The isolate was found to have a novel IMP-type metallo-β-lactamase, IMP-51, which differed from IMP-7 by an amino acid substitution (Ser262Gly). Escherichia coli expressing blaIMP-51 showed greater resistance to cefoxitin, meropenem, and moxalactam than E. coli expressing blaIMP-7. The amino acid residue at position 262 was located near the active site, proximal to the H263 Zn(II) ligand.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0066-4804eISSN: 1098-6596DOI: 10.1128/AAC.01611-15Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4604376
- Format
- –
- Schlagworte
- beta-Lactamases, beta-Lactamases - genetics, beta-Lactamases - metabolism, Carbapenems, Carbapenems - pharmacology, Cefoxitin - pharmacology, Escherichia coli, Escherichia coli - drug effects, Escherichia coli - enzymology, Mechanisms of Resistance, Microbial Sensitivity Tests, Moxalactam - pharmacology, Pseudomonas aeruginosa, Pseudomonas aeruginosa - drug effects, Pseudomonas aeruginosa - enzymology, Thienamycins, Thienamycins - pharmacology