Amyloid peptides derived from CsgA and FapC modify the viscoelastic properties of biofilm model matrices

Abstract

The bacterial biofilm is a complex environment of cells, which secrete a matrix made of various components, mainly polysaccharides and proteins. An understanding of the precise role of these components in the stability and dynamics of biofilm architecture would be a great advantage for the improvement of anti-biofilm strategies. Here, artificial biofilm matrices made of polysaccharides and auto-assembled peptides were designed, and the influence of bacterial amyloid proteins on the mechanical properties of the biofilm matrix was studied. The model polysaccharides methylcellulose and alginate and peptides derived from the amyloid proteins curli and FapC found in biofilms of Enterobacteriaceae and Pseudomonas, respectively, were used. Rheological measurements showed that the amyloid peptides do not prevent the gelation of the polysaccharides but influence deformation of the matrices under shear stress and modify the gel elastic response. Hence the secretion of amyloids could be for the biofilm a way of adapting to environmental changes.

Keywords:

• amyloid
• exopolysaccharide
• biofilm
• matrix
• viscoelastic

Acknowledgments

The authors would like to thank Alexandre Chenal from the Unité de Biochimie des Intéractions Macromoléculaires, Institut Pasteur, Paris for the FTIR experiments and Julien Picard for help with the rheology measurements and for discussion.