Fold modulating function: bacterial toxins to functional amyloids.
Fold modulating function: bacterial toxins to functional amyloids.
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DOI：
10.3389/fmicb.2014.00401
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发表时间：
2014
影响因子：
5.2
通讯作者：
Boles BR
中科院分区：
文献类型：
--
作者：
Syed AK;Boles BR
许多细菌产生靶向宿主细胞或其他竞争微生物的溶细胞毒素。众所周知，环境因素控制毒素的表达，然而，最近的工作表明，一些细菌操纵这些蛋白质毒素的折叠来控制它们的功能。富含β折叠的淀粉样蛋白折叠是许多毒素响应于特定环境条件而形成的高度稳定的有序聚集体。当处于淀粉样蛋白状态时，毒素变得惰性，失去它们以可溶形式显示的细胞溶解活性。新出现的证据表明，一些淀粉样蛋白作为毒素储存系统，直到它们再次被需要，而其他细菌利用淀粉样蛋白作为生物膜的结构基质成分。该淀粉样蛋白基质组分促进对生物膜破坏性挑战的抗性。本文中讨论的细菌淀粉样蛋白揭示了一个优雅的系统，其中蛋白质折叠和溶解度的变化决定了蛋白质响应环境的功能。
Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however, recent work suggests that some bacteria manipulate the fold of these protein toxins to control their function. The β-sheet rich amyloid fold is a highly stable ordered aggregate that many toxins form in response to specific environmental conditions. When in the amyloid state, toxins become inert, losing the cytolytic activity they display in the soluble form. Emerging evidence suggest that some amyloids function as toxin storage systems until they are again needed, while other bacteria utilize amyloids as a structural matrix component of biofilms. This amyloid matrix component facilitates resistance to biofilm disruptive challenges. The bacterial amyloids discussed in this review reveal an elegant system where changes in protein fold and solubility dictate the function of proteins in response to the environment.
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