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Characterization of metallo-beta-lactamase VIM-27, an A57S mutant of VIM-1 associated with Klebsiella pneumoniae ST147.

ABSTRACT: VIM-27 metallo-?-lactamase, an Ala(57) ? Ser variant of VIM-1, was identified in three Klebsiella pneumoniae isolates belonging to sequence type 147. bla(VIM-27) was part of a class 1 integron carried by non-self-transferable plasmids. Kinetic parameters and MIC determinations indicated that VIM-27 hydrolyzed most ?-lactams, especially imipenem and cefoxitin, less effectively than VIM-1.

SUBMITTER: Papagiannitsis CC

PROVIDER: S-EPMC3122466 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Characterization of metallo-beta-lactamase VIM-27, an A57S mutant of VIM-1 associated with Klebsiella pneumoniae ST147.

Papagiannitsis C C CC Kotsakis S D SD Petinaki E E Vatopoulos A C AC Tzelepi E E Miriagou V V Tzouvelekis L S LS

Antimicrobial agents and chemotherapy 20110425 7

VIM-27 metallo-β-lactamase, an Ala(57) → Ser variant of VIM-1, was identified in three Klebsiella pneumoniae isolates belonging to sequence type 147. bla(VIM-27) was part of a class 1 integron carried by non-self-transferable plasmids. Kinetic parameters and MIC determinations indicated that VIM-27 hydrolyzed most β-lactams, especially imipenem and cefoxitin, less effectively than VIM-1. ...[more]

PMID: 21518835

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