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.
Conference Article| July 20 2012
Exploiting amyloid: how and why bacteria use cross-β fibrils
Elizabeth B. Sawyer;
Sally L. Gras;
Sarah Perrett 1
*National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, People's Republic of China
1To whom correspondence should be addressed (firstname.lastname@example.org).
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Elizabeth B. Sawyer, Dennis Claessen, Sally L. Gras, Sarah Perrett; Exploiting amyloid: how and why bacteria use cross-β fibrils. Biochem Soc Trans 1 August 2012; 40 (4): 728–734. doi: https://doi.org/10.1042/BST20120013
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