Physical Determinants of Amyloid Assembly in Biofilm Formation.
Taylor, Jonathan D
Otzen, Daniel E
Chapman, Matthew R
Matthews, Steve J
American Society for Microbiology
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Andreasen, M., Meisl, G., Taylor, J. D., Michaels, T., Levin, A., Otzen, D. E., Chapman, M. R., et al. (2019). Physical Determinants of Amyloid Assembly in Biofilm Formation.. mBio, 10 (1)https://doi.org/10.1128/mbio.02279-18
A wide range of bacterial pathogens have been shown to form biofilms, which significantly increase their resistance to environmental stresses, such as antibi- otics, and are thus of central importance in the context of bacterial diseases. One of the major structural components of these bacterial biofilms are amyloid fibrils, yet the mechanism of fibril assembly and its importance for biofilm formation are cur- rently not fully understood. By studying fibril formation in vitro, in a model system of two common but unrelated biofilm-forming proteins, FapC from Pseudomonas fluorescens and CsgA from Escherichia coli, we found that the two proteins have a common aggregation mechanism. In both systems, fibril formation proceeds via nu- cleated growth of linear fibrils exhibiting similar measured rates of elongation, with negligible fibril self-replication. This finding suggests that convergent evolution plays a key role in tuning the assembly kinetics of functional amyloid fibrils and indicates that only a narrow window of mechanisms and assembly rates allow for successful biofilm formation. Thus, the amyloid assembly reaction is likely to represent a means for controlling biofilm formation, both by the organism and by possible inhibitory drugs.
Biofilms, Pseudomonas fluorescens, Escherichia coli, Macromolecular Substances, Amyloid, Escherichia coli Proteins, Protein Multimerization, Chemical Phenomena, Protein Aggregates
This work was supported by The Danish Council for Independent Research | Natural Sciences (FNU-11-113326) (MA), Sidney Sussex College, Cambridge (GM), the Swiss National Science Foundation and Peterhouse College, Cambridge (TCTM), The Danish Council for Independent Research | Technology and Production Sciences (6111-00241B) (DEO) National Institute of Health (R01 GM118651) (MRC), Welcome Trust Senior Investigator Award (100280) (SJM), and the Cambridge Centre for Misfolding Diseases (CMD and TPJK).
European Research Council (337969)
External DOI: https://doi.org/10.1128/mbio.02279-18
This record's URL: https://www.repository.cam.ac.uk/handle/1810/288658
Attribution 4.0 International
Licence URL: https://creativecommons.org/licenses/by/4.0/