Exploiting amyloid: how and why bacteria use cross-β fibrils

Author:

Sawyer Elizabeth B.1,Claessen Dennis2,Gras Sally L.3,Perrett Sarah1

Affiliation:

1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, People's Republic of China

2. Department of Molecular and Developmental Genetics, Institute of Biology, Leiden University, Leiden, the Netherlands

3. Department of Chemical and Biomolecular Engineering and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Australia

Abstract

Many bacteria produce protein fibrils that are structurally analogous to those associated with protein misfolding diseases such as Alzheimer's disease. However, unlike fibrils associated with disease, bacterial amyloids have beneficial functions including conferring stability to biofilms, regulating development or imparting virulence. In the present review, we consider what makes amyloid fibrils so suitable for these roles and discuss recent developments in the study of bacterial amyloids, in particular the chaplins from Streptomyces coelicolor. We also consider the broader impact of the study of bacterial amyloids on our understanding of infection and disease and on developments in nanotechnology.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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