Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / pharmacology
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Cefoxitin / pharmacology
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Drug Resistance, Multiple, Bacterial / genetics
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Imipenem / pharmacology
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Klebsiella pneumoniae / drug effects
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Klebsiella pneumoniae / enzymology*
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Klebsiella pneumoniae / genetics
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Molecular Structure
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beta-Lactamases / chemistry*
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Anti-Bacterial Agents
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Cefoxitin
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Imipenem
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VIM-1 metallo-beta-lactamase
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beta-Lactamases