TasA fibre interactions are necessary for Bacillus subtilis biofilm structure

Natalie Bamford, Ryan J. Morris, Alan Prescott, Paul Murphy, Elliot Erskine, Cait E. MacPhee (Lead / Corresponding author), Nicola Stanley-Wall (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Number of pages12
JournalMolecular Microbiology
Early online date30 Sept 2024
DOIs
Publication statusPublished - 15 Oct 2024

Keywords

  • biofilms
  • TasA
  • extracellular matrix
  • Bacillus subtilis
  • protein interactome

Fingerprint

Dive into the research topics of 'TasA fibre interactions are necessary for Bacillus subtilis biofilm structure'. Together they form a unique fingerprint.

Cite this