Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA
The soil bacterium Bacillus subtilis is a model organism to investigate the formation of biofilms, the predominant form of microbial life. The secreted protein BslA self-assembles at the surface of the biofilm to give the B. subtilis biofilm its characteristic hydrophobicity. To understand the mecha...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7615278/ https://www.ncbi.nlm.nih.gov/pubmed/37903266 http://dx.doi.org/10.1073/pnas.2312022120 |
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author | Arnaouteli, Sofia Bamford, Natalie C Brandani, Giovanni B Morris, Ryan J Schor, Marieke Carrington, Jamie T Hobley, Laura van Aalten, Daan M F Stanley-Wall, Nicola R MacPhee, Cait E |
author_facet | Arnaouteli, Sofia Bamford, Natalie C Brandani, Giovanni B Morris, Ryan J Schor, Marieke Carrington, Jamie T Hobley, Laura van Aalten, Daan M F Stanley-Wall, Nicola R MacPhee, Cait E |
author_sort | Arnaouteli, Sofia |
collection | PubMed |
description | The soil bacterium Bacillus subtilis is a model organism to investigate the formation of biofilms, the predominant form of microbial life. The secreted protein BslA self-assembles at the surface of the biofilm to give the B. subtilis biofilm its characteristic hydrophobicity. To understand the mechanism of BslA self-assembly at interfaces, here we built a molecular model based on the previous BslA crystal structure and the newly determined crystal structure of the BslA paralogue YweA. Our analysis revealed two conserved protein-protein interaction interfaces supporting BslA self-assembly into an infinite 2d lattice that fits previously determined transmission microscopy images. Molecular dynamics simulations and in vitro protein assays further support our model of BslA elastic film formation, while mutagenesis experiments highlight the importance of the identified interactions for biofilm structure. Based on this knowledge, YweA was engineered to form more stable elastic films and rescue biofilm structure in bslA deficient strains. These findings shed new light on protein film assembly and will inform the development of BslA technologies which range from surface coatings to emulsions in fast-moving consumer goods. |
format | Online Article Text |
id | pubmed-7615278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
record_format | MEDLINE/PubMed |
spelling | pubmed-76152782023-11-07 Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA Arnaouteli, Sofia Bamford, Natalie C Brandani, Giovanni B Morris, Ryan J Schor, Marieke Carrington, Jamie T Hobley, Laura van Aalten, Daan M F Stanley-Wall, Nicola R MacPhee, Cait E Proc Natl Acad Sci U S A Article The soil bacterium Bacillus subtilis is a model organism to investigate the formation of biofilms, the predominant form of microbial life. The secreted protein BslA self-assembles at the surface of the biofilm to give the B. subtilis biofilm its characteristic hydrophobicity. To understand the mechanism of BslA self-assembly at interfaces, here we built a molecular model based on the previous BslA crystal structure and the newly determined crystal structure of the BslA paralogue YweA. Our analysis revealed two conserved protein-protein interaction interfaces supporting BslA self-assembly into an infinite 2d lattice that fits previously determined transmission microscopy images. Molecular dynamics simulations and in vitro protein assays further support our model of BslA elastic film formation, while mutagenesis experiments highlight the importance of the identified interactions for biofilm structure. Based on this knowledge, YweA was engineered to form more stable elastic films and rescue biofilm structure in bslA deficient strains. These findings shed new light on protein film assembly and will inform the development of BslA technologies which range from surface coatings to emulsions in fast-moving consumer goods. 2023-11-07 2023-10-30 /pmc/articles/PMC7615278/ /pubmed/37903266 http://dx.doi.org/10.1073/pnas.2312022120 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a BY 4.0 (https://creativecommons.org/licenses/by/4.0/) International license. |
spellingShingle | Article Arnaouteli, Sofia Bamford, Natalie C Brandani, Giovanni B Morris, Ryan J Schor, Marieke Carrington, Jamie T Hobley, Laura van Aalten, Daan M F Stanley-Wall, Nicola R MacPhee, Cait E Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title | Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title_full | Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title_fullStr | Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title_full_unstemmed | Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title_short | Lateral interactions govern self-assembly of the bacterial biofilm matrix protein BslA |
title_sort | lateral interactions govern self-assembly of the bacterial biofilm matrix protein bsla |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7615278/ https://www.ncbi.nlm.nih.gov/pubmed/37903266 http://dx.doi.org/10.1073/pnas.2312022120 |
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