CTX-M-215 的进化，一种新型窄谱β-内酰胺酶，在一株对美西林耐药的大肠杆菌临床分离株中发现。
Evolution of CTX-M-215, a Novel Narrow-Spectrum β-Lactamase in an Escherichia coli Clinical Isolate Conferring Resistance to Mecillinam.
机构信息
Institute of Antibiotics, Huashan Hospital, Fudan University, Shanghai, China.
Key Laboratory of Clinical Pharmacology of Antibiotics, National Heath Commission of the People's Republic of China, Shanghai, China.
出版信息
Antimicrob Agents Chemother. 2020 Oct 20;64(11). doi: 10.1128/AAC.00562-20.
Abstract
Here, we report a novel narrow-spectrum β-lactamase CTX-M-215 identified in an clinical isolate in China and conferring high-level resistance to mecillinam but not to cefotaxime. CTX-M-215 differed from CTX-M-125, a CTX-M extended-spectrum β-lactamase (ESBL), by an N132D substitution, which decreased hydrolytic activities toward penicillins and cephalosporins except for mecillinam. High similarity was observed between CTX-M-215- and CTX-M-125-bearing plasmids, carried by different isolates in the same patient, indicating evolution of CTX-M-215 from CTX-M-125.
摘要
在这里，我们报道了一种新型的窄谱β-内酰胺酶 CTX-M-215，它存在于中国的一株临床分离株中，对氨曲南具有高水平耐药性，但对头孢噻肟没有耐药性。CTX-M-215 与 CTX-M-125（CTX-M 型超广谱β-内酰胺酶）的区别在于 N132D 取代，这降低了除氨曲南以外的青霉素类和头孢菌素类药物的水解活性。在同一患者携带的不同分离株中，CTX-M-215 携带的质粒与 CTX-M-125 携带的质粒高度相似，表明 CTX-M-215 是由 CTX-M-125 进化而来的。
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