In this section
@article{Andreasen:2019:10.1128/mBio.02279-18,
author = {Andreasen, M and Meisl, G and Taylor, JD and Michaels, TCT and Levin, A and Otzen, DE and Chapman, MR and Dobson, CM and Matthews, SJ and Knowles, TPJ},
doi = {10.1128/mBio.02279-18},
journal = {mBio},
title = {Physical determinants of amyloid assembly in biofilm formation},
url = {http://dx.doi.org/10.1128/mBio.02279-18},
volume = {10},
year = {2019}
}
TY - JOUR
AB - A wide range of bacterial pathogens have been shown to form biofilms, which significantly increase their resistance to environmental stresses, such as antibiotics, 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 currently 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 nucleated growth of linear fibrils exhibiting similar measured rates of elongation, with negligible fibril self-replication. These similarities between two unrelated systems suggest 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 allows 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.IMPORTANCE Biofilms are generated by bacteria, embedded in the formed extracellular matrix. The biofilm's function is to improve the survival of a bacterial colony through, for example, increased resistance to antibiotics or other environmental stresses. Proteins secreted by the bacteria act as a major structural component of this extracellular matrix, as they self-assemble into highly stable amyloid fibrils, making the biofilm very difficult to degrade by physical and chemical means once formed. By studying the self-assembly mechanism of the fibrils from their monomeric precursors in two unrelated bacteria, our experimental and theoretical approaches shed light on the mechanism of functional amyloid as
AU - Andreasen,M
AU - Meisl,G
AU - Taylor,JD
AU - Michaels,TCT
AU - Levin,A
AU - Otzen,DE
AU - Chapman,MR
AU - Dobson,CM
AU - Matthews,SJ
AU - Knowles,TPJ
DO - 10.1128/mBio.02279-18
PY - 2019///
SN - 2150-7511
TI - Physical determinants of amyloid assembly in biofilm formation
T2 - mBio
UR - http://dx.doi.org/10.1128/mBio.02279-18
UR - https://www.ncbi.nlm.nih.gov/pubmed/30622185
UR - http://hdl.handle.net/10044/1/77452
VL - 10
ER -
CBRB
Imperial College London
Flowers Building
Exhibition Road
London SW7 2AZ
