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BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.

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Title: BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.
Authors: Hobley, Laura1, Ostrowski, Adam1, Rao, Francesco V.1, Bromley, Keith M.2, Porter, Michael1,3, Prescott, Alan R.4, MacPhee, Cait E.2, van Aalten, Daan M. F.1,5, Stanley-Wall, Nicola R.1 n.r.stanleywall@dundee.ac.uk
Source: Proceedings of the National Academy of Sciences of the United States of America. 8/13/2013, Vol. 110 Issue 33, p13600-13605. 6p.
Subjects: Bacillus subtilis, Hydrophobins, Gram-positive bacteria, Biofilms, Microbial exopolysaccharides, Crystal structure
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. [ABSTRACT FROM AUTHOR]
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
An: 89768473
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PubTypeId: academicJournal
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  Data: BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.
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  Data: <searchLink fieldCode="AR" term="%22Hobley%2C+Laura%22">Hobley, Laura</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Ostrowski%2C+Adam%22">Ostrowski, Adam</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Rao%2C+Francesco+V%2E%22">Rao, Francesco V.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Bromley%2C+Keith+M%2E%22">Bromley, Keith M.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Porter%2C+Michael%22">Porter, Michael</searchLink><relatesTo>1,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Prescott%2C+Alan+R%2E%22">Prescott, Alan R.</searchLink><relatesTo>4</relatesTo><br /><searchLink fieldCode="AR" term="%22MacPhee%2C+Cait+E%2E%22">MacPhee, Cait E.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22van+Aalten%2C+Daan+M%2E+F%2E%22">van Aalten, Daan M. F.</searchLink><relatesTo>1,5</relatesTo><br /><searchLink fieldCode="AR" term="%22Stanley-Wall%2C+Nicola+R%2E%22">Stanley-Wall, Nicola R.</searchLink><relatesTo>1</relatesTo><i> n.r.stanleywall@dundee.ac.uk</i>
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  Data: <searchLink fieldCode="JN" term="%22Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America%22">Proceedings of the National Academy of Sciences of the United States of America</searchLink>. 8/13/2013, Vol. 110 Issue 33, p13600-13605. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Bacillus+subtilis%22">Bacillus subtilis</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrophobins%22">Hydrophobins</searchLink><br /><searchLink fieldCode="DE" term="%22Gram-positive+bacteria%22">Gram-positive bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Biofilms%22">Biofilms</searchLink><br /><searchLink fieldCode="DE" term="%22Microbial+exopolysaccharides%22">Microbial exopolysaccharides</searchLink><br /><searchLink fieldCode="DE" term="%22Crystal+structure%22">Crystal structure</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1073/pnas.1306390110
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        Text: English
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        StartPage: 13600
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      – SubjectFull: Bacillus subtilis
        Type: general
      – SubjectFull: Hydrophobins
        Type: general
      – SubjectFull: Gram-positive bacteria
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      – SubjectFull: Biofilms
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      – SubjectFull: Microbial exopolysaccharides
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      – SubjectFull: Crystal structure
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      – TitleFull: BslA is a self-assembling bacterial hydrophobin that coats the Bacillus subtilis biofilm.
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              Text: 8/13/2013
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