Komatsu Y, Murakami K, Nishikawa T
Antimicrob Agents Chemother. 1981 Nov;20(5):613-9. doi: 10.1128/AAC.20.5.613.
An eschericia coli K-12 mutant highly resistant to moxalactam but only slightly resistant to other beta-lactam antibiotics was obtained by mutagen treatment. The affinity of moxalactam for its target penicillin-binding proteins was unchanged, as was the level of beta-lactamase activity. The penetration of [14C] moxalactam, however, was markedly reduced in the mutant. Electrophoretic analysis revealed alterations of the outer membrane proteins. A reduction in the amount of one of the pore-forming proteins (porins) was especially noteworthy. These data suggest that moxalactam resistance is the result of an alteration in the outer membrane structure.
通过诱变处理获得了一株对莫西拉坦高度耐药但对其他β-内酰胺类抗生素仅轻度耐药的大肠杆菌K-12突变体。莫西拉坦与其靶标青霉素结合蛋白的亲和力未发生变化，β-内酰胺酶活性水平也未改变。然而，[14C]莫西拉坦在该突变体中的渗透明显降低。电泳分析显示外膜蛋白发生了改变。其中一种形成孔道的蛋白（孔蛋白）数量减少尤其值得注意。这些数据表明，莫西拉坦耐药性是外膜结构改变的结果。
