Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor

McCaughey, LC; Grinter, R; Josts, I; Roszak, AW; Waløen, KI; Cogdell, RJ; Milner, J; Evans, T; Kelly, S; Tucker, NP; Byron, O; Smith, B; Walker, D

Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor

Grinter, R Josts, I Roszak, AW Waløen, KI Cogdell, RJ Milner, J Evans, T Kelly, S Tucker, NP Byron, O Smith, B Walker, D

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Publication Type:: Journal Article
Citation:: PLoS Pathogens, 2014, 10 (2)
Issue Date:: 2014-01-01

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Field	Value	Language
dc.contributor.author	McCaughey, LC https://orcid.org/0000-0001-5897-0163	en_US
dc.contributor.author	Grinter, R	en_US
dc.contributor.author	Josts, I	en_US
dc.contributor.author	Roszak, AW	en_US
dc.contributor.author	Waløen, KI	en_US
dc.contributor.author	Cogdell, RJ	en_US
dc.contributor.author	Milner, J	en_US
dc.contributor.author	Evans, T	en_US
dc.contributor.author	Kelly, S	en_US
dc.contributor.author	Tucker, NP	en_US
dc.contributor.author	Byron, O	en_US
dc.contributor.author	Smith, B	en_US
dc.contributor.author	Walker, D	en_US
dc.date.available	2013-12-10	en_US
dc.date.issued	2014-01-01	en_US
dc.identifier.citation	PLoS Pathogens, 2014, 10 (2)	en_US
dc.identifier.issn	1553-7366	en_US
dc.identifier.uri	http://hdl.handle.net/10453/58784
dc.description.abstract	Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-specific killing activity. Here we show that pyocin L1, a novel member of this family from Pseudomonas aeruginosa, targets susceptible strains of this species through recognition of the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide that is predominantly a homopolymer of <sc>d</sc>-rhamnose. Structural and biophysical analyses show that recognition of CPA occurs through the C-terminal carbohydrate-binding domain of pyocin L1 and that this interaction is a prerequisite for bactericidal activity. Further to this, we show that the previously described lectin-like bacteriocin putidacin L1 shows a similar carbohydrate-binding specificity, indicating that oligosaccharides containing <sc>d</sc>-rhamnose and not <sc>d</sc>-mannose, as was previously thought, are the physiologically relevant ligands for this group of bacteriocins. The widespread inclusion of <sc>d</sc>-rhamnose in the lipopolysaccharide of members of the genus Pseudomonas explains the unusual genus-specific activity of the lectin-like bacteriocins. © 2014 McCaughey et al.	en_US
dc.relation.ispartof	PLoS Pathogens	en_US
dc.relation.isbasedon	10.1371/journal.ppat.1003898	en_US
dc.subject.classification	Virology	en_US
dc.subject.mesh	Pseudomonas aeruginosa	en_US
dc.subject.mesh	Rhamnose	en_US
dc.subject.mesh	Lipopolysaccharides	en_US
dc.subject.mesh	Bacteriocins	en_US
dc.subject.mesh	Immunoblotting	en_US
dc.subject.mesh	Mutagenesis, Site-Directed	en_US
dc.subject.mesh	Polymerase Chain Reaction	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Structure, Quaternary	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.title	Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	10	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	1107 Immunology	en_US
utslib.for	1108 Medical Microbiology	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	open_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	10	en_US

Abstract:

Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-specific killing activity. Here we show that pyocin L1, a novel member of this family from Pseudomonas aeruginosa, targets susceptible strains of this species through recognition of the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide that is predominantly a homopolymer of d-rhamnose. Structural and biophysical analyses show that recognition of CPA occurs through the C-terminal carbohydrate-binding domain of pyocin L1 and that this interaction is a prerequisite for bactericidal activity. Further to this, we show that the previously described lectin-like bacteriocin putidacin L1 shows a similar carbohydrate-binding specificity, indicating that oligosaccharides containing d-rhamnose and not d-mannose, as was previously thought, are the physiologically relevant ligands for this group of bacteriocins. The widespread inclusion of d-rhamnose in the lipopolysaccharide of members of the genus Pseudomonas explains the unusual genus-specific activity of the lectin-like bacteriocins. © 2014 McCaughey et al.

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http://hdl.handle.net/10453/58784