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Updated: May 25, 2026

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Published on: May 4, 2018
IMP-29, a novel IMP-type metallo-β-lactamase in Pseudomonas aeruginosa
Katy Jeannot1, Laurent Poirel, Marjorie Robert-Nicoud
1Centre National de la Résistance aux Antibiotiques, Laboratoire associé Pseudomonas aeruginosa, Hôpital Jean Minjoz, Besançon, France.
Abstract:
Analysis of two clonally related multiresistant Pseudomonas aeruginosa isolates led to the identification of a novel IMP-type metallo-β-lactamase. IMP-29 was significantly different from the other IMP variants (the closest variant being IMP-5 with 93% amino acid identity). The bla(IMP-29) gene cassette was carried by a class 1 integron in strain 10.298, while in strain 10.266 it was located in a rearranged DNA region on a 30-kb conjugative plasmid. Biochemical analysis confirmed that IMP-29 efficiently hydrolyzed carbapenems.
Insights
Researchers discovered a new metallo-beta-lactamase, IMP-29, in multidrug-resistant Pseudomonas aeruginosa. This enzyme efficiently breaks down carbapenems, a critical class of antibiotics, raising concerns for antimicrobial resistance.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Multidrug resistance in Pseudomonas aeruginosa poses a significant global health threat.
- Metallo-beta-lactamases (MBLs) are a class of enzymes conferring resistance to carbapenems, a last-resort antibiotic class.
- Emergence of novel MBL variants necessitates continuous surveillance and characterization.
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