Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 33, Pages 13600-13605Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1306390110
Keywords
biofilm surface protein; in situ immunofluorescence; biofilm hydrophobicity
Categories
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/C520404/1, BB/I019464/1]
- BBSRC Doctoral Training Account Grant [BB/D526161/1]
- Federation of European Biochemical Societies (FEBS) Return-to-Europe Fellowship
- Marie Curie European Research Council International Re-Integration Grant (ERC-IRG) [IRG26838]
- Medical Research Council Programme Grant [G0900138]
- Wellcome Trust [WT087590MA, 083524/Z/07/Z]
- Biotechnology and Biological Sciences Research Council [BB/C520404/1, BB/I019464/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J007404/1] Funding Source: researchfish
- Medical Research Council [G0900138] Funding Source: researchfish
- BBSRC [BB/I019464/1] Funding Source: UKRI
- EPSRC [EP/J007404/1] Funding Source: UKRI
- MRC [G0900138] Funding Source: UKRI
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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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