{"database":"ENA","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Fastqsanger.gz":["ftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/008/ERR3453498/ERR3453498_2.fastq.gz","ftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/009/ERR3453499/ERR3453499_2.fastq.gz","ftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/008/ERR3453498/ERR3453498_1.fastq.gz","ftp://ftp.sra.ebi.ac.uk/vol1/fastq/ERR345/009/ERR3453499/ERR3453499_1.fastq.gz"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Genomics"],"center_name":["Lausanne University Hospital","laboratory of genomics and metagenomics, institute of microbiology, university hospital centre and university of lausanne, switzerland"],"full_dataset_link":["https://www.ebi.ac.uk/ena/browser/view/PRJEB33694"],"tag":["xref:EuropePMC:PMC6879233"],"long_description":["This 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."],"repository":["ENA"],"additional_accession":[]},"is_claimable":false,"name":"","description":"A novel KPC variant, KPC-41, was identified in a Klebsiella pneumoniae clinical isolate from Switzerland.","dates":{"last_updated":"2019-07-26","first_public":"2019-07-25"},"accession":"PRJEB33694","cross_references":{}}