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Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly
Authors:Maya Deshmukh  Margery L. Evans  Matthew R. Chapman
Affiliation:Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, 1105 N University Ave, Ann Arbor, MI 48109-1085, USA
Abstract: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.
Keywords:ThT  thioflavin-T  curli-specific gene  PSMα3  phenol-soluble modulin α3  functional amyloid  protein misfolding  microbial amyloids  nature-inspired therapeutics  toxic oligomer
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