KILLING OF CANDIDA-ALBICANS BY LACTOFERRICIN-B, A POTENT ANTIMICROBIAL PEPTIDE DERIVED FROM THE N-TERMINAL REGION OF BOVINE LACTOFERRIN
KILLING OF CANDIDA-ALBICANS BY LACTOFERRICIN-B, A POTENT ANTIMICROBIAL PEPTIDE DERIVED FROM THE N-TERMINAL REGION OF BOVINE LACTOFERRIN
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DOI：
10.1007/bf00189377
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发表时间：
1993-05-01
影响因子：
5.4
通讯作者：
TOMITA, M
中科院分区：
文献类型：
--
作者：
BELLAMY, W;WAKABAYASHI, H;TOMITA, M
白色念珠菌被发现对乳铁蛋白B的抑制和失活非常敏感，乳铁蛋白B是一种由牛乳铁蛋白酶切产生的肽。肽的有效浓度在18至150马克杯/毫升的范围内变化，这取决于菌株和使用的培养基。它的影响是致命的，导致群体形成能力的迅速丧失。c -14标记的乳铁蛋白B与白色念珠菌结合，结合率与肽诱导的杀伤率一致。在Mg2+或Ca2+离子的存在下，结合程度降低，这降低了其抗药效果。在pH为6.0时结合效果最佳，而在接近相同pH时杀伤效果最大。这些证据表明乳铁蛋白B的致死作用是由其与细胞表面的直接相互作用引起的。暴露于乳铁蛋白B的细胞表现出深刻的超微结构损伤，这似乎反映了其诱导的自溶反应。这些发现表明，乳铁蛋白活性肽可能有助于宿主防御白色念珠菌。
Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 mug/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. C-14-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.