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

DOI: 10.1371/journal.ppat.1003898 DOI Help
PMID: 24516380 PMID Help

Authors: Laura C. Mccaughey (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Rhys Grinter (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Inokentijs Josts (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Aleksander Roszak (University of Glasgow) , Kai I. Wal√łen (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Richard J. Cogdell (Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary, and Life Sciences, University of Glasgow) , Joel Milner (Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary, and Life Sciences, University of Glasgow,) , Tom Evans (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Sharon Kelly (Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary, and Life Sciences, University of Glasgow) , Nicholas P. Tucker (Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde) , Olwyn Byron (University of Glasgow) , Brian Smith (Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary, and Life Sciences, University of Glasgow) , Daniel Walker (Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos Pathogens , VOL 10 (2)

State: Published (Approved)
Published: February 2014
Diamond Proposal Number(s): 6683

Open Access Open Access

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.

Journal Keywords: Bacteriocins ; Immunoblotting ; Lipopolysaccharides ; Mutagenesis ; Site-Directed ; Polymerase; Protein; Quaternary ; Pseudomonas; Rhamnose

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Documents:
journal.ppat.1003898.pdf