<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.
Authors
- Cait E. MacPhee (ORCID: https://orcid.org/0000-0001-8313-8387)
- Elliot Erskine
- Natalie C. Bamford (ORCID: https://orcid.org/0000-0003-1959-856X)
- Alan R. Prescott (ORCID: https://orcid.org/0000-0002-0747-7317)
- Nicola R. Stanley‐Wall (ORCID: https://orcid.org/0000-0002-5936-9721)
- Ryan J. Morris (ORCID: https://orcid.org/0000-0003-4764-3639)
- Paul Murphy
Institutions
- University of Dundee (GB)
- Edinburgh Cancer Research (GB)
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
Funders
- European Molecular Biology Organization
- University of Dundee
- Wellcome Trust
- Medical Research Council
- Biotechnology and Biological Sciences Research Council