Extended-Spectrum Cephalosporinase in Acinetobacter baumannii
Copyright policy )Extended-Spectrum Cephalosporinase in Acinetobacter baumannii
ABSTRACT An AmpC-type β-lactamase conferring high-level resistance to expanded-spectrum cephalosporins and monobactams was characterized from an Acinetobacter baumannii clinical isolate. This class C β-lactamase (named ADC-33) possessed a Pro210Arg substitution together with a duplication of an Ala residue at position 215 (inside the Ω-loop) compared to a reference AmpC cephalosporinase from A. baumannii . ADC-33 hydrolyzed ceftazidime, cefepime, and aztreonam at high levels, which allows the classification of this enzyme as an extended-spectrum AmpC (ESAC). Site-directed mutagenesis confirmed the role of both substitutions in its ESAC property.
- Panthéon-Assas University France
- University of Paris France
- University of Paris-Sud France
- Hopital Raymond Poincaré France
Acinetobacter baumannii, Cephalosporin Resistance, Molecular Sequence Data, Microbial Sensitivity Tests, Ceftazidime, beta-Lactamases, Anti-Bacterial Agents, Cephalosporins, Aztreonam, Amino Acid Substitution, Bacterial Proteins, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Cefepime, Cephalosporinase, Monobactams
Acinetobacter baumannii, Cephalosporin Resistance, Molecular Sequence Data, Microbial Sensitivity Tests, Ceftazidime, beta-Lactamases, Anti-Bacterial Agents, Cephalosporins, Aztreonam, Amino Acid Substitution, Bacterial Proteins, Mutagenesis, Site-Directed, Humans, Amino Acid Sequence, Cefepime, Cephalosporinase, Monobactams
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