BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm
Data(s) |
13/08/2013
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Resumo |
<p>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.</p> |
Identificador | |
Idioma(s) |
eng |
Direitos |
info:eu-repo/semantics/restrictedAccess |
Fonte |
Hobley , L , Ostrowski , A , Rao , F V , Bromley , K M , Porter , M , Prescott , A R , MacPhee , C E , van Aalten , D M F & Stanley-Wall , N R 2013 , ' BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm ' Proceedings of the National Academy of Sciences of the United States of America , vol 110 , no. 33 , pp. 13600-5 . DOI: 10.1073/pnas.1306390110 |
Palavras-Chave | #Bacillus subtilis #Bacterial Proteins #Biofilms #Biophysics #Fluorescent Antibody Technique #Hydrophobic and Hydrophilic Interactions #Microscopy, Confocal #Models, Molecular #Protein Conformation |
Tipo |
article |