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Microbial functional amyloids serve diverse purposes for structure, adhesion and defence

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Abstract

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.

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Correspondence to Margaret Sunde.

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MS is funded by the Australian Research Council (DP180101275). NS, MODGB and SRB are supported by the Research Training Program of the Australian Government.

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Nirukshan Shanmugam declares that he has no conflict of interest. Max O. D. G. Baker declares that he has no conflict of interest. Sarah R. Ball declares that she has no conflict of interest. Megan Steain declares that she has no conflict of interest. Chi L. L. Pham declares that she has no conflict of interest. Margaret Sunde declares that she has no conflict of interest.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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This article is part of a Special Issue dedicated to the ‘2018 Joint Conference of the Asian Biophysics Association and Australian Society for Biophysics’ edited by Kuniaki Nagayama, Raymond Norton, Kyeong Kyu Kim, Hiroyuki Noji, Till Böcking and Andrew Battle.

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Shanmugam, N., Baker, M.O.D.G., Ball, S.R. et al. Microbial functional amyloids serve diverse purposes for structure, adhesion and defence. Biophys Rev 11, 287–302 (2019). https://doi.org/10.1007/s12551-019-00526-1

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  • DOI: https://doi.org/10.1007/s12551-019-00526-1

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