Pfm-like enzymes are a novel family of subclass b2 metallo-β-lactamases from Pseudomonas synxantha belonging to the Pseudomonas fluorescens complex
Poirel, LaurentMicrobiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland - INSERM European Unit (IAME, France), University of Fribourg, Fribourg, Switzerland - Swiss National Reference Center for Emerging Antibiotic Resistance (NARA), University of Fribourg, Switzerland
Palmieri, MattiaMicrobiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland - bioMérieux, Data Analytics Unit, La Balme Les Grottes, France
Brilhante, MichaelInstitute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Switzerland
Masseron, AmandineMicrobiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland
Perreten, VincentInstitute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Switzerland
Nordmann, PatriceMicrobiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland - INSERM European Unit (IAME, France), University of Fribourg, Fribourg, Switzerland - Swiss National Reference Center for Emerging Antibiotic Resistance (NARA), University of Fribourg, Switzerland - Institute for Microbiology, University of Lausanne and University Hospital Centre, Lausanne, Switzerland
Antimicrobial Agents and Chemotherapy. - 2020, vol. 64, no. 2, p. 10.1128/aac.01700-19
English
A carbapenem-resistant Pseudomonas synxantha isolate recovered from chicken meat produced the novel carbapenemase PFM-1. That subclass B2 metallo-β- lactamase shared 71% amino acid identity with β-lactamase Sfh-1 from Serratia fonticola. The blaPFM-1 gene was chromosomally located and likely acquired. Variants of PFM-1 sharing 90% to 92% amino acid identity were identified in bacterial species belonging to the Pseudomonas fluorescens complex, including Pseudomonas libanensis (PFM-2) and Pseudomonas fluorescens (PFM-3), highlighting that these species constitute reservoirs of PFM-like encoding genes.