Biophysical Reviews

, Volume 11, Issue 3, pp 287–302 | Cite as

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

  • Nirukshan Shanmugam
  • Max O. D. G. Baker
  • Sarah R. Ball
  • Megan Steain
  • Chi L. L. Pham
  • Margaret SundeEmail author


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.


Functional amyloid Fibrils Biofilm Curli RHIM Hydrophobin 


Compliance with ethical standards

Funding information

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

Conflict of interest

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.

Ethical approval

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


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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Discipline of Pharmacology, School of Medical Sciences, Faculty of Medicine and Health and Sydney NanoUniversity of SydneySydneyAustralia
  2. 2.Infectious Diseases and Immunology, Central Clinical School, Sydney Medical SchoolUniversity of SydneySydneyAustralia

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