DECREASED AFFINITY OF A PENICILLIN-BINDING PROTEIN FOR BETA-LACTAM ANTIBIOTICS IN A CLINICAL ISOLATE OF STAPHYLOCOCCUS-AUREUS RESISTANT TO METHICILLIN
DECREASED AFFINITY OF A PENICILLIN-BINDING PROTEIN FOR BETA-LACTAM ANTIBIOTICS IN A CLINICAL ISOLATE OF STAPHYLOCOCCUS-AUREUS RESISTANT TO METHICILLIN
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DOI：
10.1111/j.1574-6968.1981.tb06220.x
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发表时间：
1981-01-01
影响因子：
2.1
通讯作者：
WARD, JB
中科院分区：
文献类型：
--
作者：
HAYES, MV;CURTIS, NAC;WARD, JB
耐甲氧西林（MR）金黄色葡萄球菌菌株的特点是对许多青霉素和头孢菌素具有耐药性[1]。甲氧西林耐药性（通常称为“内在耐药性”）的生化基础尚不清楚，但似乎与可检测到的抗生素酶失活无关，尽管此类菌株经常产生β-内酰胺酶[2-4]。13-内酰胺抗生素被认为通过抑制膜结合的“致命”靶标青霉素来杀死细菌。结合蛋白 (PBP)[5] 被认为可以催化肽聚糖生物合成的末端反应 [6]。最近，修饰的 PBP 被认为是 13-1actam 耐药性的机制。例如，大肠杆菌 K-12 的一些耐美西林突变体具有修饰的 PBP2，其对该抗生素的亲和力降低 [7]，并且 PBP 的改变似乎与氯唑西林相关
Methicillin-resistant (MR) strains of Staphylococcus aureus are characterised by their resistance to many penicillins and cephalosporins [1]. The biochemical basis for methicillin resistance, often termed" intrinsic resistance", is not known but appears to be independant of detectable enzymic inactivation of the ant~ iotic, even though such strains often produce~-lactamase [2-4].13-Lactam antibiotics are believed to kill bacteria by inhibiting membrane bound" lethal" target Penicillin. Binding Proteins (PBPs)[5] which are thought to catalyse the terminal reactions of peptidoglycan biosynthesis [6]. Modified PBPs have recently been implicated as a mechanism of 13-1actam resistance. For example, some mecillinarn-resistant mutants of Escherichia coli K-12 have a modified PBP2 with decreased affinity for that antibiotic [7] and alterations in PBPs appeared to correlated with cloxacillin