Studies on Serum Resistance in E scherichia coli

Britta S. Kubens, Wolfgang Opferkuch
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引用次数: 5

Abstract

Serum-sensitive mutants and their serum-resistant smooth parental E. coli strains (Wf8, Wf26, and WF 52) have been investigated in respect to their binding of different complement components. These pairs consisting of a wild-type and its mutants represent a better model for the investigation of the mechanism of serum resistance than the comparison of unrelated strains. Both strains of a pair bind equivalent amounts of C3. In binding assays using radiolabeled terminal components C6, C7, C8, and C9, the serum-sensitive strains do bind more late acting components than their resistant parental strains. An active membrane attack complex stably bound to the cell surface was found on the mutants, whereas with wild-type bacteria a complex could be isolated from the supernatant which is composed of the late acting complement components and S-protein. This complex is released from the surface of the wild-type bacteria without participation of C9.

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大肠杆菌血清耐药性研究
研究了血清敏感突变体及其血清耐药平滑亲本大肠杆菌菌株(Wf8、Wf26和wf52)与不同补体成分的结合情况。这些由野生型及其突变体组成的菌株对血清耐药机制的研究比不相关菌株的比较更好。一对中的两株结合等量的C3。在使用放射标记的末端组分C6、C7、C8和C9的结合试验中,血清敏感菌株确实比它们的抗性亲本菌株结合更多的晚期作用组分。在突变体上发现了一个稳定结合在细胞表面的活性膜攻击复合物,而在野生型细菌上清中可以分离到一个由晚期补体成分和s蛋白组成的复合物。这种复合物在没有C9参与的情况下从野生型细菌表面释放出来。
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