Biochemical characterization of VIM-39, a VIM-1-like metallo-β-lactamase variant from a multidrug-resistant Klebsiella pneumoniae isolate from Greece

Costas C. Papagiannitsis, Simona Pollini, Filomena De Luca, Gian Maria Rossolini, Jean Denis Docquier, Jaroslav Hrabák

Research output: Contribution to journalArticlepeer-review

Abstract

VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates.

Original languageEnglish
Pages (from-to)7811-7814
Number of pages4
JournalAntimicrobial Agents and Chemotherapy
Volume59
Issue number12
DOIs
Publication statusPublished - Dec 1 2015

ASJC Scopus subject areas

  • Pharmacology (medical)
  • Pharmacology
  • Infectious Diseases

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