Service de Bactériologie-Virologie, INSERM U914 Emerging Resistance to Antibiotics, Assistance Publique/Hôpital de Paris, Faculté deMédecine and Université Paris-Sud, France.
Antimicrob Agents Chemother. 2010 Aug;54(8):3484-8. doi: 10.1128/AAC.00050-10. Epub 2010 Jun 14.
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.
从鲍曼不动杆菌临床分离株中鉴定出一种 AmpC 型β-内酰胺酶,对广谱头孢菌素类和单环β-内酰胺类药物具有高水平耐药性。与鲍曼不动杆菌的参考 AmpC 头孢菌素酶相比,这种 C 类β-内酰胺酶(命名为 ADC-33)在 210 位脯氨酸取代的同时,在 215 位(ω环内)的丙氨酸残基发生了重复。ADC-33 高水平水解头孢他啶、头孢吡肟和氨曲南,因此可将该酶归类为扩展谱 AmpC(ESAC)。定点突变证实了这两个取代在其 ESAC 特性中的作用。