Abertay Research Collections >
Research Centres >
SIMBIOS Collection >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10373/197

View Statistics
Title: Biofilm formation at the air–liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose
Authors: Spiers, Andrew J.
Bohannon, John
Gehrig, Stefanie M.
Rainey, Paul B.
Affiliation: University of Abertay Dundee. Scottish Informatics, Mathematics, Biology and Statistics Centre
Keywords: Biofilms
Issue Date: Oct-2003
Publisher: Blackwell Publishing Ltd
Type: Journal Article
Refereed: peer-reviewed
Rights: Published version (c)Blackwell Publishing Ltd. For full bibliographic citation please refer to the version available at www3.interscience.wiley.com
Citation: Spiers, A. J., et al. 2003. Biofilm formation at the air–liquid interface by the Pseudomonas fluorescens SBW25 wrinkly spreader requires an acetylated form of cellulose. Molecular Microbiology. 50(1): pp.15-27. [Onine] Available from: DOI: 10.1046/j.1365-2958.2003.03670.x
Abstract: The wrinkly spreader (WS) genotype of Pseudomonas fluorescens SBW25 colonizes the air–liquid interface of spatially structured microcosms resulting in formation of a thick biofilm. Its ability to colonize this niche is largely due to overproduction of a cellulosic polymer, the product of the wss operon. Chemical analysis of the biofilm matrix shows that the cellulosic polymer is partially acetylated cellulose, which is consistent with predictions of gene function based on in silico analysis of wss. Both polar and non-polar mutations in the sixth gene of the wss operon (wssF ) or adjacent downstream genes (wssGHIJ ) generated mutants that overproduce non-acetylated cellulose, thus implicating WssFGHIJ in acetylation of cellulose. WssGHI are homologues of AlgFIJ from P. aeruginosa, which together are necessary and sufficient to acetylate alginate polymer. WssF belongs to a newly established Pfam family and is predicted to provide acyl groups to WssGHI. The role of WssJ is unclear, but its similarity to MinD-like proteins suggests a role in polar localization of the acetylation complex. Fluorescent microscopy of Calcofluor-stained biofilms revealed a matrix structure composed of networks of cellulose fibres, sheets and clumped material. Quantitative analyses of biofilm structure showed that acetylation of cellulose is important for effective colonization of the air–liquid interface: mutants identical to WS, but defective in enzymes required for acetylation produced biofilms with altered physical properties. In addition, mutants producing non-acetylated cellulose were unable to spread rapidly across solid surfaces. Inclusion in these assays of a WS mutant with a defect in the GGDEF regulator (WspR) confirmed the requirement for this protein in expression of both acetylated cellulose polymer and bacterial attachment. These results suggest a model in which WspR regulation of cellulose expression and attachment plays a role in the co-ordination of surface colonization.
URI: http://hdl.handle.net/10373/197
ISSN: 0950-382X
Appears in Collections:SIMBIOS Collection

Files in This Item:

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback