Spread of st348 klebsiella pneumoniae producing NDM-1 in a peruvian hospital

Maria J. Pons, Marta Marí-Almirall, Barbara Ymaña, Jeel Moya-Salazar, Laura Muñoz, Sharon Sauñe, Richard Salazar-Hernández, Jordi Vila, Ignasi Roca

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12 Scopus citations

Abstract

The aim of this study was to characterize carbapenem-resistant Klebsiella pneumoniae (CR-Kp) isolates recovered from adults and children with severe bacteremia in a Peruvian Hospital in June 2018. Antimicrobial susceptibility was determined by disc/gradient diffusion and broth microdilution when necessary. Antibiotic resistance mechanisms were evaluated by PCR and DNA sequencing. Clonal relatedness was assessed using pulsed-field gel electrophoresis (PFGE) and multilocus sequence typing (MLST). Plasmid typing was performed with a PCR-based method. Thirty CR-Kp isolates were recovered in June 2018. All isolates were non-susceptible to all β-lactams, ciprofloxacin, gentamicin and trimethoprim-sulfamethoxazole, while mostly remaining susceptible to colistin, tigecycline, levofloxacin and amikacin. All isolates carried the blaNDM-1 gene and were extended spectrum β-lactamase (ESBL) producers. PFGE showed four different pulsotypes although all isolates but two belonged to the ST348 sequence type, previously reported in Portugal. blaNDM-1 was located in an IncFIB-M conjugative plasmid. To our knowledge, this is the first report of an New Delhi metallo-β-lactamase (NDM)-producing K. pneumoniae recovered from both children and adults in Lima, Peru, as well as the first time that the outbreak strain ST348 is reported in Peru and is associated with NDM. Studies providing epidemiological and molecular data on CR-Kp in Peru are essential to monitor their dissemination and prevent further spread.

Original languageEnglish
Article number1392
Pages (from-to)1-10
Number of pages10
JournalMicroorganisms
Volume8
Issue number9
DOIs
StatePublished - Sep 2020

Keywords

  • Bloodstream infections
  • Carbapenem resistance
  • Epidemiology
  • Klebsiella pneumoniae
  • Metallo-β-lactamase

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