克洛辛DF13在体外与纯化的外膜受体蛋白的结合以及肽聚糖对细菌素-受体相互作用的影响。
In vitro binding of cloacin DF13 to its purified outer membrane receptor protein and effect of peptidoglycan on bacteriocin-receptor interaction.
作者信息
Oudega B, van der Molen J, de Graaf F K
出版信息
J Bacteriol. 1979 Dec;140(3):964-70. doi: 10.1128/jb.140.3.964-970.1979.
Abstract
The in vitro neutralization of the killing activity of cloacin DF13 by incubation with its purified receptor protein was shown to be the result of the formation of a direct and specific equimolar complex of both proteins. The binding of cloacin DF13 to its receptor protein did not result in a fragmentation of the cloacin molecules nor in the expulsion of immunity protein from the bacteriocin. The rate of the cloacin DF13-receptor interaction in vitro was found to be enhanced significantly in the presence of peptidoglycan, but lysozyme-treated peptidoglycan did not affect this interaction. Incubation of the cloacin DF13 as well as its receptor protein with peptidoglycan showed that the receptor protein but not the cloacin DF13 was able to bind to the peptidoglycan.
摘要
通过与纯化的受体蛋白孵育，可实现对杀鱼菌素DF13杀伤活性的体外中和，这是两种蛋白形成直接且特异性等摩尔复合物的结果。杀鱼菌素DF13与其受体蛋白的结合既不会导致杀鱼菌素分子的断裂，也不会使免疫蛋白从细菌素中排出。发现在肽聚糖存在的情况下，杀鱼菌素DF13与受体的体外相互作用速率显著提高，但经溶菌酶处理的肽聚糖不影响这种相互作用。将杀鱼菌素DF13及其受体蛋白与肽聚糖一起孵育表明，能够与肽聚糖结合的是受体蛋白而非杀鱼菌素DF13。
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