Microbial functional amyloids serve diverse purposes for structure, adhesion and defence
Autor: | Chi L.L. Pham, Margaret Sunde, Megan Steain, Sarah R. Ball, Nirukshan Shanmugam, Max O.D.G. Baker |
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Rok vydání: | 2019 |
Předmět: |
0303 health sciences
Amyloid Hydrophobin Biophysics Membrane biology Biofilm Review Computational biology Biology 010402 general chemistry Pathogenicity 01 natural sciences 0104 chemical sciences Aberrant protein 03 medical and health sciences chemistry.chemical_compound chemistry Structural Biology mental disorders Thioflavin Fibrillar morphology Molecular Biology 030304 developmental biology |
Zdroj: | Biophysical Reviews. 11:287-302 |
ISSN: | 1867-2469 1867-2450 |
DOI: | 10.1007/s12551-019-00526-1 |
Popis: | The functional amyloid state of proteins has in recent years garnered much attention for its role in serving crucial and diverse biological roles. Amyloid is a protein fold characterised by fibrillar morphology, binding of the amyloid-specific dyes Thioflavin T and Congo Red, insolubility and underlying cross-β structure. Amyloids were initially characterised as an aberrant protein fold associated with mammalian disease. However, in the last two decades, functional amyloids have been described in almost all biological systems, from viruses, to bacteria and archaea, to humans. Understanding the structure and role of these amyloids elucidates novel and potentially ancient mechanisms of protein function throughout nature. Many of these microbial functional amyloids are utilised by pathogens for invasion and maintenance of infection. As such, they offer novel avenues for therapies. This review examines the structure and mechanism of known microbial functional amyloids, with a particular focus on the pathogenicity conferred by the production of these structures and the strategies utilised by microbes to interfere with host amyloid structures. The biological importance of microbial amyloid assemblies is highlighted by their ubiquity and diverse functionality. |
Databáze: | OpenAIRE |
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