<scp>TasA</scp> Fibre Interactions Are Necessary for <i>Bacillus subtilis</i> Biofilm Structure

The extracellular matrix of biofilms provides crucial structural support to the community and protection from environmental perturbations. TasA, a key Bacillus subtilis biofilm matrix protein, forms both amyloid and non-amyloid fibrils. Non-amyloid TasA fibrils are formed via a strand-exchange mechanism, whereas the amyloid-like form involves non-specific self-assembly. We performed mutagenesis of the N-terminus to assess the role of non-amyloid fibrils in biofilm development. We find that the N-terminal tail is essential for the formation of structured biofilms, providing evidence that the strand-exchange fibrils are the active form in the biofilm matrix. Furthermore, we demonstrate that fibre formation alone is not sufficient to give structure to the biofilm. We build an interactome of TasA with other extracellular protein components, and identify important interaction sites. Our results provide insight into how protein-matrix interactions modulate biofilm development.

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Publication Details

Journal
Molecular Microbiology
Published
2024-09-30
DOI
https://doi.org/10.1111/mmi.15315
Citations
6
Primary Topic
Bacterial biofilms and quorum sensing
Type
article
Field-Weighted Citation Impact
1.40

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article

TasA Fibre Interactions Are Necessary for Bacillus subtilis Biofilm Structure

Cait E. MacPhee, Elliot Erskine, Natalie C. Bamford, Alan R. Prescott et al.
6 citations
Molecular Microbiology
Bacterial biofilms and quorum sensing
1.40
article

TasA Fibre Interactions Are Necessary for Bacillus subtilis Biofilm Structure

Cait E. MacPhee, Elliot Erskine, Natalie C. Bamford, Alan R. Prescott, Nicola R. Stanley‐Wall, Ryan J. Morris, Paul Murphy
article en
6 citations

Abstract

The extracellular matrix of biofilms provides crucial structural support to the community and protection from environmental perturbations. TasA, a key Bacillus subtilis biofilm matrix protein, forms both amyloid and non-amyloid fibrils. Non-amyloid TasA fibrils are formed via a strand-exchange mechanism, whereas the amyloid-like form involves non-specific self-assembly. We performed mutagenesis of the N-terminus to assess the role of non-amyloid fibrils in biofilm development. We find that the N-terminal tail is essential for the formation of structured biofilms, providing evidence that the strand-exchange fibrils are the active form in the biofilm matrix. Furthermore, we demonstrate that fibre formation alone is not sufficient to give structure to the biofilm. We build an interactome of TasA with other extracellular protein components, and identify important interaction sites. Our results provide insight into how protein-matrix interactions modulate biofilm development.

Molecular MicrobiologyVol. 122(4)
University of Dundee (GB), Edinburgh Cancer Research (GB)
European Molecular Biology Organization, University of Dundee, Wellcome Trust, Medical Research Council, Biotechnology and Biological Sciences Research Council
Life in Land
Openalex Percentile: Top 19%
Bacterial biofilms and quorum sensing
1.40
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