ENAapplication/xmlftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/008/ERR3453498/ERR3453498_2.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/009/ERR3453499/ERR3453499_2.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/008/ERR3453498/ERR3453498_1.fastq.gzftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/009/ERR3453499/ERR3453499_1.fastq.gzprimaryOK200GenomicsLausanne University Hospitallaboratory of genomics and metagenomics, institute of microbiology, university hospital centre and university of lausanne, switzerlandhttps://www.ebi.ac.uk/ena/browser/view/PRJEB33694xref:EuropePMC:PMC6879233This beta-lactamase possessed a three amino acid insertion (Pro-Asn-Lys) located between amino acids 269 and 270 compared to the KPC-3 amino acid sequence. Cloning and expression of the blaKPC-41 gene in Escherichia coli, followed by determination of MIC values and kinetic parameters showed that KPC-41 has an increased affinity to ceftazidime and a decreased sensitivity to avibactam, leading to resistance to ceftazidime-avibactam once produced in K. pneumoniae. Furthermore, KPC-41 exhibited a drastic decrease of its carbapenemase activity. This report highlights that a diversity of KPC variants conferring resistance to ceftazidime-avibactam already circulate in Europe.ENAfalseA novel KPC variant, KPC-41, was identified in a Klebsiella pneumoniae clinical isolate from Switzerland.2019-07-262019-07-25PRJEB33694