Characterization of OXA-204, a Carbapenem-Hydrolyzing Class D β-Lactamase from Klebsiella pneumoniae
Author(s) -
Anaïs Potron,
Patrice Nordmann,
Laurent Poirel
Publication year - 2012
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.01034-12
Subject(s) - klebsiella pneumoniae , transposition (logic) , plasmid , microbiology and biotechnology , carbapenem , enterobacteriaceae , klebsiella , insertion sequence , gene , biology , escherichia coli , antibiotics , transposable element , genetics , genome , linguistics , philosophy
AKlebsiella pneumoniae clinical isolate recovered in Tunisia showed resistance to all β-lactams and decreased susceptibility to carbapenems.K. pneumoniae 204 expressed the carbapenem-hydrolyzing β-lactamase OXA-204, differing from OXA-48 by two amino acid substitutions (Gln98His and Thr99Arg) (class D β-lactamase [DBL] numbering). OXA-48 and OXA-204 shared similar resistance profiles, hydrolyzing carbapenems but sparing broad-spectrum cephalosporins. Thebla OXA-204 gene was located on a ca. 150-kb IncA/C-type plasmid, which also carried thebla CMY-4 gene. Thebla OXA-204 gene was associated with an ISEcp1 element, whereas thebla OXA-48 genes are usually associated with IS1999 .
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