细胞结合在乳铁蛋白B抗菌机制中的作用。

The Journal of applied bacteriology Pub Date : 1993-11-01
W R Bellamy, H Wakabayashi, M Takase, K Kawase, S Shimamura, M Tomita
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引用次数: 0

摘要

首次研究了从牛乳铁蛋白中提取的强效抗菌肽乳铁蛋白B的抗菌细胞结合特性。为了方便结合的测量,通过还原和碘-[1-14C]乙酰胺处理对肽进行放射性标记。14c -乳铁蛋白B能迅速与大肠杆菌和枯草芽孢杆菌表面结合。结合速度与该肽引起的快速杀伤速度一致。在Mg2+或Ca2+离子的存在下,结合程度降低,从而降低其抗菌效果。各菌株的最佳结合pH值与菌株有关,在最佳结合pH附近杀伤效果最大。这些观察结果表明,乳铁蛋白B与细胞表面的直接相互作用是其致死作用所必需的。结合的肽分子数量(每个细胞> 10(6))比预期的与特定蛋白质受体结合的多。乳铁蛋白B抑制细菌摄取3h -脯氨酸的效果与多粘菌素B相似,多粘菌素B是一种已知的膜破坏剂。细胞结合事件似乎导致细胞质膜正常通透功能的破坏。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Role of cell-binding in the antibacterial mechanism of lactoferricin B.

The antibacterial cell-binding properties of lactoferricin B, a potent bactericidal peptide derived from bovine lactoferrin, were investigated for the first time. To facilitate measurements of binding the peptide was radiolabelled by reduction and treatment with iodo-[1-14C]acetamide. 14C-lactoferricin B bound rapidly to the surface of Escherichia coli and Bacillus subtilis. The rate of binding was consistent with the rapid rate of killing caused by this peptide. The extent of binding was reduced in the presence of Mg2+ or Ca2+ ions which act to reduce its antimicrobial effectiveness. The optimal pH for binding was strain-dependent and the killing effect was maximal near the optimal pH for cell binding with each strain tested. These observations indicate that direct interaction of lactoferricin B with the cell surface is necessary for its lethal effect. The number of peptide molecules bound (> 10(6) per cell) was more than would be expected for binding to specific protein receptors. Lactoferricin B inhibited bacterial uptake of 3H-proline with effectiveness similar to polymyxin B, a known membrane-disruptive agent. The cell-binding event appears to lead to a disruption of normal permeability functions of the cytoplasmic membrane.

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