Institute of Medical Microbiology, Virology and Hygiene, University Medical Centre Hamburg-Eppendorf, Hamburg, Germany.
Microb Drug Resist. 2011 Jun;17(2):165-9. doi: 10.1089/mdr.2010.0137. Epub 2011 Mar 9.
We isolated a clinical Escherichia coli strain with an antimicrobial resistance phenotype characteristic for the expression of an AmpC beta-lactamase. Molecular methods revealed a novel, plasmid-localized variant of CMY-2 with a substitution of valine 231 for serine (V231S), which was designated CMY-42. Like the CMY-2-like AmpC beta-lactamase CMY-30, carrying the substitution V231G, CMY-42 displayed increased activity toward expanded spectrum cephalosporins. This finding supports the hypothesis that a bulky side chain at position 231 (Ambler's position 211) may pose a steric clash with certain cephalosporins hindering the access of the AmpC beta-lactamase; however, additional phenomena may account for the observed hydrolytic properties.
我们分离出一株具有抗菌表型的临床型大肠杆菌,其特征是表达一种 AmpC 型β-内酰胺酶。分子方法揭示了一种新型的、质粒定位的 CMY-2 变体,其缬氨酸 231 被丝氨酸取代(V231S),被命名为 CMY-42。与携带取代 V231G 的 CMY-2 样 AmpC 型β-内酰胺酶 CMY-30 一样,CMY-42 对扩展谱头孢菌素的活性增加。这一发现支持了这样一种假设,即在位置 231(安布勒位置 211)处的大侧链可能与某些头孢菌素发生空间冲突,阻碍 AmpC 型β-内酰胺酶的进入;然而,可能还有其他现象解释了观察到的水解特性。