The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
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DOI：
10.1016/j.jmb.2005.07.028
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发表时间：
2005-09-16
影响因子：
5.6
通讯作者：
Gazit, E
中科院分区：
文献类型：
--
作者：
Cherny, I;Rockah, L;Gazit, E
淀粉样原纤维形成是包括阿尔茨海默病、II型糖尿病和朊病毒疾病在内的主要人类疾病的标志。在酵母中也观察到朊病毒样现象。虽然在进化上没有相关性，但动物PrP和酵母Sup 35朊病毒蛋白之间的一个相似之处是短肽重复序列的出现，这些短肽重复序列被认为在淀粉样蛋白结构的组装中起关键作用。最近证实，典型的淀粉样纤维形成与大肠杆菌生物膜形成有关。在这里，我们注意到的主要curli蛋白和动物和酵母朊病毒的寡肽重复序列之间的功能和结构相似性。我们证明，合成肽对应的重复形成纤维状结构。此外，β-破坏因子与朊病毒样重复序列的缀合显著抑制淀粉样蛋白形成和表达卷曲蛋白的细菌的细胞侵袭。这意味着重复在原纤维的自组装中的功能作用。由于哺乳动物朊病毒，酵母朊病毒和curli蛋白是进化上不同的，保守的肽重复序列最有可能定义一个优化的自缔合基序，独立地演变的不同系统。(c)2005爱思唯尔有限公司保留所有权利。
Amyloid fibril formation is the hallmark of major human maladies including Alzheimer's disease, type II diabetes, and prion diseases. Prion-like phenomena were also observed in yeast. Although not evolutionarily related, one similarity between the animal PrP and the yeast Sup35 prion proteins is the occurrence of short peptide repeats that are assumed to play a key role in the assembly of the amyloid structures. It was recently demonstrated that typical amyloid fibril formation is associated with biofilm formation by Escherichia coli. Here, we note the functional and structural similarity between oligopeptide repeats of the major curli protein and those of animal and yeast prions. We demonstrate that synthetic peptides corresponding to the repeats form fibrillar structures. Furthermore, conjugation of beta-breaker elements to the prion-like repeat significantly inhibits amyloid formation and cell invasion of curli-expressing bacteria. This implies a functional role of the repeat in the self-assembly of the fibrils. Since mammal prion, yeast prion, and curli protein are evolutionarily distinct, the conserved peptide repeats most likely define an optimized self-association motif that was independently evolved by diverse systems. (c) 2005 Elsevier Ltd. All rights reserved.