Service de Bactériologie-Virologie, INSERM U914, Emerging Resistance to Antibiotics, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.
Antimicrob Agents Chemother. 2011 Jan;55(1):349-54. doi: 10.1128/AAC.00773-10. Epub 2010 Oct 18.
Acinetobacter baumannii isolate AP was recovered from a bronchial lavage of a patient hospitalized in Paris, France. A. baumannii AP was resistant to all β-lactams, including carbapenems, and produced the extended-spectrum β-lactamase (ESBL) GES-14, which differs from GES-1 by two substitutions, Gly170Ser and Gly243Ala. Cloning of the bla(GES-14) gene followed by its expression in Escherichia coli showed that GES-14 compromised significantly the efficacy of all β-lactams, including cephalosporins, aztreonam, and carbapenems. The carbapenemase activity of purified GES-14 was confirmed by kinetic studies. The bla(GES-14) gene was located into a class 1 integron structure and located onto a ca. 95-kb self-transferable plasmid. This study identified a very broad-spectrum β-lactamase in A. baumannii.
鲍曼不动杆菌分离株 AP 从一名在法国巴黎住院的患者的支气管灌洗液中分离得到。AP 对所有β-内酰胺类药物（包括碳青霉烯类药物）均具有耐药性，并产生了超广谱β-内酰胺酶（ESBL）GES-14，该酶与 GES-1 相比有两个取代，即 Gly170Ser 和 Gly243Ala。克隆 bla(GES-14) 基因并在大肠杆菌中表达后，结果表明 GES-14 显著降低了所有β-内酰胺类药物（包括头孢菌素类、氨曲南和碳青霉烯类药物）的疗效。通过动力学研究证实了纯化的 GES-14 的碳青霉烯酶活性。bla(GES-14) 基因位于类 1 整合子结构中，并位于一个约 95kb 的可自我转移的质粒上。本研究鉴定了鲍曼不动杆菌中的一种非常广谱的β-内酰胺酶。
