ArticleProceedings of the National Academy of Sciences of the United States of America2013
BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 140 papers.
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Who cites it
140 citing papers in PubMed.
- Integrated functional genomics and safety assessment of plant-growth-promoting Caryophanales from post-maize-cultivation soils.BMC genomics · 2026Article
- Molecular mechanisms and applications of antimicrobial secondary metabolites ofApplied and environmental microbiology · 2026Review
- MeeY and YybP, two proteins regulated by manganese-sensing riboswitches, are required for Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2026Article
- Genomic and transcriptomic analysis of yield enhancement mechanism of lipopeptide iturin W by tryptone supplementation.Microbiology spectrum · 2026Article
- Effect of biofilm lifestyle caused by water matric potential on invasion of exogenous plasmid.ISME communications · 2026Article
- Draft genome sequence of a chromium-resistant Bacillus altitudinis AK25 strain isolated from contaminated aquatic environment.BMC genomic data · 2025Article
- Biofilm structure as a key factor in antibiotic tolerance: insights from Bacillus subtilis model systems.NPJ biofilms and microbiomes · 2025Article
- PrtA-mediated flagellar turnover is essential for robust biofilm development inApplied and environmental microbiology · 2025Article
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- The biofilm matrix protectsBiofilm · 2025Article
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- Time-resolved compositional and dynamics analysis of biofilm maturation and dispersal via solid-state NMR spectroscopy.NPJ biofilms and microbiomes · 2025Article
- Bacterial osmoprotectants-a way to survive in saline conditions and potential crop allies.FEMS microbiology reviews · 2025Review
- Adaptive laboratory evolution for improved tolerance of vitamin K in Bacillus subtilis.Applied microbiology and biotechnology · 2024Article
- Bacillus subtilis EpsA-O: A novel exopolysaccharide structure acting as an efficient adhesive in biofilms.NPJ biofilms and microbiomes · 2024Article
- How bacteria actively use passive physics to make biofilms.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mobility and growth in confined spaces are important mechanisms for the establishment ofMicrobiology (Reading, England) · 2024Article
- Characterization and genome mining ofHeliyon · 2024Article
- Role of Bacillus subtilis exopolymeric genes in modulating rhizosphere microbiome assembly.Environmental microbiome · 2024Article
80 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
Abstract
Biofilms represent the predominant mode of microbial growth in the natural environment. Bacillus subtilis is a ubiquitous Gram-positive soil bacterium that functions as an effective plant growth-promoting agent. The biofilm matrix is composed of an exopolysaccharide and an amyloid fiber-forming protein, TasA, and assembles with the aid of a small secreted protein, BslA. Here we show that natively synthesized and secreted BslA forms surface layers around the biofilm. Biophysical analysis demonstrates that BslA can self-assemble at interfaces, forming an elastic film. Molecular function is revealed from analysis of the crystal structure of BslA, which consists of an Ig-type fold with the addition of an unusual, extremely hydrophobic "cap" region. A combination of in vivo biofilm formation and in vitro biophysical analysis demonstrates that the central hydrophobic residues of the cap are essential to allow a hydrophobic, nonwetting biofilm to form as they control the surface activity of the BslA protein. The hydrophobic cap exhibits physiochemical properties remarkably similar to the hydrophobic surface found in fungal hydrophobins; thus, BslA is a structurally defined bacterial hydrophobin. We suggest that biofilms formed by other species of bacteria may have evolved similar mechanisms to provide protection to the resident bacterial community.
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