Carbapenem-Hydrolyzing GES-Type Extended-Spectrum β-Lactamase in Acinetobacter baumannii
Carbapenem-Hydrolyzing GES-Type Extended-Spectrum β-Lactamase in Acinetobacter baumannii
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DOI：
10.1128/aac.00773-10
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发表时间：
2011-01-01
影响因子：
4.9
通讯作者：
Poirel, Laurent
中科院分区：
文献类型：
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作者：
Bonnin, Remy A.;Nordmann, Patrice;Poirel, Laurent
鲍曼不动杆菌分离AP是从法国巴黎住院的一名患者的支气管灌洗中分离出来的。鲍曼不动杆菌AP对包括碳青霉烯类在内的所有β -内酰胺类均具有抗性，产生的广谱β -内酰胺酶（ESBL） GES-14与GES-1存在Gly170Ser和Gly243Ala两个取代基的差异。bla（GES-14）基因的克隆和在大肠杆菌中的表达表明，GES-14显著降低了所有β -内酰胺类药物的疗效，包括头孢菌素、氨曲南和碳青霉烯类药物。通过动力学研究证实了纯化的GES-14的碳青霉烯酶活性。bla（gs -14）基因位于1类整合子结构中，位于约95 kb的可自转移质粒上。本研究在鲍曼不动杆菌中鉴定出一种广谱β -内酰胺酶。
Acinetobacter baumannii isolate AP was recovered from a bronchial lavage of a patient hospitalized in Paris, France. A. baumannii AP was resistant to all beta-lactams, including carbapenems, and produced the extended-spectrum beta-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 beta-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 beta-lactamase in A. baumannii.