Journal article

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

EB Sawyer, D Claessen, SL Gras, S Perrett

Biochemical Society Transactions | PORTLAND PRESS LTD | Published : 2012

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 nanotech..

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University of Melbourne Researchers

Grants

Awarded by National Natural Science Foundation of China


Awarded by Chinese Ministry of Science and Technology


Awarded by Chinese Academy of Sciences


Funding Acknowledgements

Work in the Perrett laboratory is supported by the National Natural Science Foundation of China [grant numbers 30870482, 31070656 and 31110103914], the Chinese Ministry of Science and Technology [grant number 2012CB911000] and the Chinese Academy of Sciences [grant numbers KSCX2-YW-R-119 and KSCX2-YW-R-256]. In addition, E.B.S. is supported by a Chinese Academy of Sciences Fellowship for Young International Scientists [grant number 2010Y2SB01] and the National Natural Science Foundation of China [grant number 31150110150].