Antibacterial mechanism of bifidocin A, a novel broad-spectrum bacteriocin produced by Bifidobacterium animalis BB04
Antibacterial mechanism of bifidocin A, a novel broad-spectrum bacteriocin produced by Bifidobacterium animalis BB04
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动物双歧杆菌 BB04 产生的新型广谱细菌素双歧杆菌素 A 的抗菌机制
DOI：
10.1016/j.foodcont.2015.10.033
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发表时间：
2016-04-01
期刊：
影响因子：
6
通讯作者：
Sun, Baoguo
中科院分区：
文献类型：
--
作者：
Liu, Guorong;Song, Zhenqin;Sun, Baoguo
双歧杆菌A是从健康百岁老人粪便中分离得到的一种新型广谱细菌素。为了解双歧杆菌A对革兰氏阴性菌的抑菌作用机制，研究了双歧杆菌A在最低抑菌浓度下对大肠杆菌1.90细胞形态、胞内组织、膜通透性、膜完整性和膜质子动力（PMF）的影响。扫描电镜和透射电镜分析表明，双歧杆菌A诱导了E. coil细胞形态和细胞内组织的改变。细胞内组织比形态更容易受到双歧杆菌A的影响。双双霉素A处理引起了IC+和无机磷酸盐的泄漏，ATP和紫外线吸收物质的释放，E. coil细胞的跨膜电位和pH梯度的崩溃。共聚焦激光扫描显微镜图像显示双歧杆菌A处理的线圈细胞吸收了碘化丙啶。这些结果表明，双歧杆菌A对大肠杆菌的作用机制涉及细胞质膜PMF的耗散，膜通透性增加，细胞膜形成孔，膜完整性改变，细胞完全解体。(C) 2015 Elsevier Ltd.版权所有。
Bifidocin A, a novel broad-spectrum bacteriocin produced by Bffidobacterium animalis BB04, was isolated from the feces of a healthy centenarian. To understand the mechanism of the antibacterial action of bifidocin A against gram-negative bacteria, its effects at a minimum inhibitory concentration on cell morphology, intracellular organization, membrane permeability, membrane integrity, and membrane proton motive force (PMF) of Escherichia coli 1.90 were investigated. Scanning and transmission electron microscopy analyses showed that bifidocin A induced alterations in the morphology and intracellular organization of E. coil cells. The intracellular organization was more susceptible to changes induced by bifidocin A than the morphology. Bifidocin A treatment caused the leakage of IC+ and inorganic phosphate, the release of ATP and UV-absorbing materials, and a collapse of the transmembrane electrical potential and pH gradient in E. coil cells. Confocal laser scanning microscopy images showed that E. coil cells treated with bifidocin A took up propidium iodide. These results suggested that the mechanism of action bifidocin A against E. coil involved dissipation of the PMF of the cytoplasmic membrane, an increase in membrane permeability, pore formation in the cell membrane, a change in membrane integrity, and complete cell disintegration. (C) 2015 Elsevier Ltd. All rights reserved.