Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly

被引:40
作者
Deshmukh, Maya [1 ]
Evans, Margery L. [1 ]
Chapman, Matthew R. [1 ]
机构
[1] Univ Michigan, Dept Mol Cellular & Dev Biol, 1105 N Univ Ave, Ann Arbor, MI 48109 USA
基金
美国国家卫生研究院;
关键词
functional amyloid; protein misfolding; microbial amyloids; nature-inspired therapeutics; toxic oligomer; SOLID-STATE NMR; RESOLUTION 3-DIMENSIONAL STRUCTURE; FUNGUS PODOSPORA-ANSERINA; ESCHERICHIA-COLI O157-H7; PAIRED HELICAL FILAMENTS; BIOFILM FORMATION; ALPHA-SYNUCLEIN; SECONDARY NUCLEATION; HETEROKARYON INCOMPATIBILITY; FIBRONECTIN-BINDING;
D O I
10.1016/j.jmb.2018.07.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The term amyloid has historically been used to describe fibrillar aggregates formed as the result of protein misfolding and that are associated with a range of diseases broadly termed amyloidoses. The discovery of "functional amyloids" expanded the amyloid umbrella to encompass aggregates structurally similar to disease-associated amyloids but that engage in a variety of biologically useful tasks without incurring toxicity. The mechanisms by which functional amyloid systems ensure nontoxic assembly has provided insights into potential therapeutic strategies for treating amyloidoses. Some of the most-studied functional amyloids are ones produced by bacteria. Curli amyloids are extracellular fibers made by enteric bacteria that function to encase and protect bacterial communities during biofilm formation. Here we review recent studies highlighting microbial functional amyloid assembly systems that are tailored to enable the assembly of non-toxic amyloid aggregates. (C) 2018 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3631 / 3641
页数:11
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