Extended-spectrum cephalosporinase in Acinetobacter baumannii.

Article Details

Citation

Rodriguez-Martinez JM, Nordmann P, Ronco E, Poirel L

Extended-spectrum cephalosporinase in Acinetobacter baumannii.

Antimicrob Agents Chemother. 2010 Aug;54(8):3484-8. doi: 10.1128/AAC.00050-10. Epub 2010 Jun 14.

PubMed ID
20547808 [ View in PubMed
]
Abstract

An AmpC-type beta-lactamase conferring high-level resistance to expanded-spectrum cephalosporins and monobactams was characterized from an Acinetobacter baumannii clinical isolate. This class C beta-lactamase (named ADC-33) possessed a Pro210Arg substitution together with a duplication of an Ala residue at position 215 (inside the Omega-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.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
CefotaximeBeta-lactamaseProteinAcinetobacter baumannii
Unknown
Not AvailableDetails