Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae

Pierre Bogaerts; Carine Bebrone; Te-Din Huang; Warda Bouchahrouf; Yves Degheldre; Ariane Deplano; Kurt Hoffmann; Youri Glupczynski

doi:10.1128/AAC.06249-11

Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae

Antimicrob Agents Chemother. 2012 Jun;56(6):3283-7. doi: 10.1128/AAC.06249-11. Epub 2012 Mar 5.

Authors

Pierre Bogaerts¹, Carine Bebrone, Te-Din Huang, Warda Bouchahrouf, Yves Degheldre, Ariane Deplano, Kurt Hoffmann, Youri Glupczynski

Affiliation

¹ Laboratory of Bacteriology, CHU Mont-Godinne, Université Catholique de Louvain, Yvoir, Belgium.

Abstract

We report the first description of the metallo-β-lactamase VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in Enterobacter cloacae 11236, which was isolated from blood specimens of a patient with colonic adenocarcinoma in Belgium. bla(VIM-31) was found on a class 1 integron located on a self-transferable but not typeable 42-kb plasmid. Compared to values published elsewhere for VIM-2, the purified VIM-31 enzyme showed weaker catalytic efficiency against all the tested beta-lactam agents (except for ertapenem), resulting from lower k(cat) (except for ertapenem) and higher K(m) values for VIM-31.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Electrophoresis, Gel, Pulsed-Field
Electroporation
Enterobacter cloacae / enzymology*
Kinetics
Molecular Sequence Data
Mutation
Polymerase Chain Reaction
beta-Lactamases / genetics*

Substances

beta-Lactamases

Associated data

GENBANK/JN982330