PFM-Like Enzymes Are a Novel Family of Subclass B2 Metallo-β-Lactamases from Pseudomonas synxantha Belonging to the Pseudomonas fluorescens Complex.
Détails
ID Serval
serval:BIB_DD20E8636D5A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
PFM-Like Enzymes Are a Novel Family of Subclass B2 Metallo-β-Lactamases from Pseudomonas synxantha Belonging to the Pseudomonas fluorescens Complex.
Périodique
Antimicrobial agents and chemotherapy
ISSN
1098-6596 (Electronic)
ISSN-L
0066-4804
Statut éditorial
Publié
Date de publication
27/01/2020
Peer-reviewed
Oui
Volume
64
Numéro
2
Pages
e01700-19
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Publication Status: epublish
Résumé
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 bla <sub>PFM-1</sub> 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.
Mots-clé
Amino Acid Sequence, Anti-Bacterial Agents/metabolism, Anti-Bacterial Agents/pharmacology, Bacterial Proteins/chemistry, Bacterial Proteins/genetics, Carbapenems/metabolism, Carbapenems/pharmacology, Drug Resistance, Bacterial/genetics, Drug Resistance, Multiple, Bacterial/genetics, Escherichia coli/metabolism, Kinetics, Microbial Sensitivity Tests, Pseudomonas/drug effects, Pseudomonas/enzymology, Pseudomonas fluorescens/drug effects, Pseudomonas fluorescens/enzymology, beta-Lactamases/biosynthesis, beta-Lactamases/chemistry, beta-Lactamases/classification, beta-Lactamases/genetics, PFM-1, Pseudomonas fluorescens, metallo-beta-lactamase
Pubmed
Web of science
Open Access
Oui
Création de la notice
05/12/2020 16:23
Dernière modification de la notice
10/02/2024 7:15