首页> 外文期刊>International journal of infectious diseases : >Poblational and biochemical-structural analyses on CTX-M @b-lactamases harboring the D240G mutation reveal that E. coli populations with decreased susceptibility to ceftazidime preexist under a multifactorial resistance profile
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Poblational and biochemical-structural analyses on CTX-M @b-lactamases harboring the D240G mutation reveal that E. coli populations with decreased susceptibility to ceftazidime preexist under a multifactorial resistance profile

机译:对带有D240G突变的CTX-M @ b-内酰胺酶的基础和生化结构分析表明,在多因素耐药情况下,对头孢他啶敏感性下降的大肠杆菌种群已存在

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Purpose: CTX-M β-lactamases possess high catalytic efficiency towards cefotaxime (CTX) but spare ceftazidime (CAZ). Variants harboring the replacement of D240 by a glycine (D240G substitution) have been associated with a decreased susceptibility to CAZ. We analyzed the influence of D240G, and spontaneous porin deficient subpopulations in the five CTX-M sub families in relation to final MICs.
机译:目的:CTX-Mβ-内酰胺酶对头孢噻肟(CTX)具有较高的催化效率,但对头孢他啶(CAZ)具有多余的催化作用。带有甘氨酸替代D240的变体(D240G替代)与降低对CAZ的敏感性有关。我们分析了D240G的影响以及与最终MIC相关的五个CTX-M亚家族中自发性孔蛋白缺陷型亚群的影响。

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