Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA

• DOI: 10.1073/pnas.2312022120
• Publication Date: 2023-10-30T19:09:20Z
• Authors: Sofia Arnaouteli; Natalie C. Bamford; Giovanni B. Brandani; Ryan J. Morris; Marieke Schor; Jamie T. Carrington; Laura Hobley; Daan M. F. van Aa...; Nicola R. Stanley...; Cait E. MacPhee
• Keywords: Bacterial Proteins; Extracellular Polymeric Substance Matrix; Biofilms; protein assemblies; Biological Sciences; Molecular Dynamics Simulation; biofilm matrix; molecular dynamic simulations; X-ray crystallography; Bacillus subtilis

The soil bacterium Bacillus subtilis is a model organism to investigate the formation of biofilms, predominant form microbial life. secreted protein BslA self-assembles at surface biofilm give B. its characteristic hydrophobicity. To understand mechanism self-assembly interfaces, here we built molecular based on previous crystal structure and paralogue YweA that determined. Our analysis revealed two conserved protein–protein interaction interfaces supporting into an infinite 2-dimensional lattice fits previously determined transmission microscopy images. Molecular dynamics simulations in vitro assays further support our elastic film formation, while mutagenesis experiments highlight importance identified interactions for structure. Based this knowledge, was engineered more stable films rescue bslA deficient strains. These findings shed light assembly will inform development technologies which range from coatings emulsions fast-moving consumer goods.