Journal article
+ 1 other files
Chromobacterium spp. harbour Ambler class A β-lactamases showing high identity with KPC
-
Gudeta, Dereje Dadi
Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg, Denmark
-
Bortolaia, Valeria
Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg, Denmark
-
Jayol, Aurélie
Medical and Molecular Microbiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland
-
Poirel, Laurent
Medical and Molecular Microbiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland
-
Nordmann, Patrice
Medical and Molecular Microbiology Unit, Department of Medicine, Faculty of Science, University of Fribourg, Switzerland - HFR—Hôpital Cantonal, Fribourg, Switzerland
-
Guardabassi, Luca
Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Frederiksberg, Denmark - Department of Biomedical Sciences, Ross University School of Veterinary Medicine, St Kitts, West Indies
Show more…
Published in:
- Journal of Antimicrobial Chemotherapy. - 2016, vol. 71, no. 6, p. 1493-1496
English
Objectives The origin of KPC is unknown. The aim of this study was to detect progenitors of KPC in silico and to functionally verify their β-lactam hydrolysis activity.Methods The sequence of KPC-2 was used to mine the NCBI protein sequence database. The best non-KPC hits were analysed by amino acid (aa) alignment and phylogenetic tree construction. Genes encoding KPC-2 homologues were expressed in Escherichia coli. The carbapenemase activities of the recombinant strains were characterized by the CarbaNP test and UV spectrophotometry and MICs of selected β-lactams were determined.Results Genes encoding the closest KPC-2 homologues were identified on the chromosome of Chromobacterium piscinae strain ND17 (CRP-1, 76% aa identity), Chromobacterium sp. C-61 (CRS-1, 70% aa identity) and Chromobacterium haemolyticum DSM19808 (CRH-1, 69% aa identity). All three Chromobacterium β-lactamases were phylogenetically more related to KPC than to other Ambler class A β-lactamases. The 27 bp region preceding the start codon of blaCRP-1 displayed high nucleotide identity to the corresponding region upstream from blaKPC (74%). Heterologous expression of blaCRP-1 and to a lesser extent of blaCRH-1 in E. coli significantly increased the MICs of meropenem and most cephalosporins. The CarbaNP test was positive for both recombinant strains, but spectrophotometric analysis confirmed higher carbapenemase activity for CRP-1-producing clones.Conclusions The recovery of three class A β-lactamases with up to 76% aa identity to KPC from distinct Chromobacterium species is highly indicative of the role played by this genus in the evolution of KPC.
-
Faculty
- Faculté des sciences et de médecine
-
Department
- Médecine 3ème année
-
Language
-
-
Classification
-
Biological sciences
-
License
-
License undefined
-
Identifiers
-
-
Persistent URL
-
https://folia.unifr.ch/unifr/documents/304715
Other files
Statistics
Document views: 27
File downloads:
- nor_cha.pdf: 55
- nor_cha_sm.pdf: 51