Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1

Nouwens, AS; Beatson, SA; Whitchurch, CB; Walsh, BJ; Schweizer, HP; Mattick, JS; Cordwell, SJ

Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1

Nouwens, AS Beatson, SA Whitchurch, CB

Walsh, BJ Schweizer, HP Mattick, JS Cordwell, SJ

Permalink

Publication Type:: Journal Article
Citation:: Microbiology, 2003, 149 (5), pp. 1311 - 1322
Issue Date:: 2003-05-01

Closed Access

	Filename	Description	Size
	2008000879OK.pdf		479.14 kB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Nouwens, AS	en_US
dc.contributor.author	Beatson, SA	en_US
dc.contributor.author	Whitchurch, CB https://orcid.org/0000-0003-2296-3791	en_US
dc.contributor.author	Walsh, BJ	en_US
dc.contributor.author	Schweizer, HP	en_US
dc.contributor.author	Mattick, JS	en_US
dc.contributor.author	Cordwell, SJ	en_US
dc.date.issued	2003-05-01	en_US
dc.identifier.citation	Microbiology, 2003, 149 (5), pp. 1311 - 1322	en_US
dc.identifier.issn	1350-0872	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8631
dc.description.abstract	The las and rhl quorum sensing (QS) systems regulate the expression of several genes in response to cell density changes in Pseudomonas aeruginosa. Many of these genes encode surface-associated or secreted virulence factors. Proteins from stationary phase culture supernatants were collected from wild-type and P. aeruginosa PAO1 mutants deficient in one or more of the lasRI, rhlRI and vfr genes and analysed using two-dimensional gel electrophoresis. All mutants released significantly lower amounts of protein than the wild-type. Protein spot patterns from each strain were compared using image analysis and visible spot differences were identified using mass spectrometry. Several previously unknown QS-regulated proteins were characterized, including an aminopeptidase (PA2939), an endoproteinase (PrpL) and a unique 'hypothetical' protein (PA0572), which could not be detected in the culture supernatants of Δlas mutants, although they were unaffected in Δrhl mutants. Chitin-binding protein (CbpD) and a hypothetical protein (PA4944) with similarity to host factor I (HF-I) could not be detected when any of the lasRI or rhlRI genes were disrupted. Fourteen proteins were present at significantly greater levels in the culture supernatants of QS mutants, suggesting that QS may also negatively control the expression of some genes. Increased levels of two-partner secretion exoproteins (PA0041 and PA4625) were observed and may be linked to increased stability of their cognate transporters in a QS-defective background. Known QS-regulated extracellular proteins, including elastase (lasB), LasA protease lasA) and alkaline metalloproteinase (aprA) were also detected.	en_US
dc.relation.ispartof	Microbiology	en_US
dc.relation.isbasedon	10.1099/mic.0.25967-0	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Pseudomonas aeruginosa	en_US
dc.subject.mesh	Ligases	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	DNA-Binding Proteins	en_US
dc.subject.mesh	Trans-Activators	en_US
dc.subject.mesh	Proteome	en_US
dc.subject.mesh	Transcription Factors	en_US
dc.subject.mesh	Cyclic AMP Receptor Protein	en_US
dc.subject.mesh	Electrophoresis, Gel, Two-Dimensional	en_US
dc.subject.mesh	Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization	en_US
dc.subject.mesh	Gene Expression Regulation, Bacterial	en_US
dc.subject.mesh	Mutation	en_US
dc.title	Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1	en_US
dc.type	Journal Article
utslib.citation.volume	5	en_US
utslib.citation.volume	149	en_US
utslib.for	0605 Microbiology	en_US
dc.location.activity	ISI:000183033000023	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.issue	5	en_US
pubs.publication-status	Published	en_US
pubs.volume	149	en_US

Abstract:

The las and rhl quorum sensing (QS) systems regulate the expression of several genes in response to cell density changes in Pseudomonas aeruginosa. Many of these genes encode surface-associated or secreted virulence factors. Proteins from stationary phase culture supernatants were collected from wild-type and P. aeruginosa PAO1 mutants deficient in one or more of the lasRI, rhlRI and vfr genes and analysed using two-dimensional gel electrophoresis. All mutants released significantly lower amounts of protein than the wild-type. Protein spot patterns from each strain were compared using image analysis and visible spot differences were identified using mass spectrometry. Several previously unknown QS-regulated proteins were characterized, including an aminopeptidase (PA2939), an endoproteinase (PrpL) and a unique 'hypothetical' protein (PA0572), which could not be detected in the culture supernatants of Δlas mutants, although they were unaffected in Δrhl mutants. Chitin-binding protein (CbpD) and a hypothetical protein (PA4944) with similarity to host factor I (HF-I) could not be detected when any of the lasRI or rhlRI genes were disrupted. Fourteen proteins were present at significantly greater levels in the culture supernatants of QS mutants, suggesting that QS may also negatively control the expression of some genes. Increased levels of two-partner secretion exoproteins (PA0041 and PA4625) were observed and may be linked to increased stability of their cognate transporters in a QS-defective background. Known QS-regulated extracellular proteins, including elastase (lasB), LasA protease lasA) and alkaline metalloproteinase (aprA) were also detected.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/8631