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Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly
- Source :
- Journal of Molecular Biology. 430:3631-3641
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
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.
- Subjects :
- 0301 basic medicine
Amyloid
Protein Folding
Cell Survival
Enteric bacteria
Protein Aggregation, Pathological
Article
Protein Aggregates
Structure-Activity Relationship
03 medical and health sciences
Assembly systems
Bacterial Proteins
Structural Biology
mental disorders
Animals
Humans
Protein Interaction Domains and Motifs
Molecular Biology
030102 biochemistry & molecular biology
Protein Stability
Chemistry
Biofilm
Amyloidosis
Cell biology
030104 developmental biology
Protein folding
Protein Multimerization
Function (biology)
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 430
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....88ebb1fd9724f333e636e62f81afa3f8
- Full Text :
- https://doi.org/10.1016/j.jmb.2018.07.007