Publication

Article Metrics

Citations


Online attention

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 (University of Glasgow) , Rhys Grinter (University of Glasgow) , Inokentijs Josts (University of Glasgow) , Aleksander Roszak (University of Glasgow) , Kai I. Waløen (University of Glasgow) , Richard J. Cogdell (University of Glasgow) , Joel Milner (University of Glasgow) , Tom Evans (University of Glasgow) , Sharon Kelly (University of Glasgow) , Nicholas P. Tucker (University of Strathclyde) , Olwyn Byron (University of Glasgow) , Brian Smith (University of Glasgow) , Daniel Walker (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; Lectins; Pseudomonas aeruginosa; Polysaccharides; Pseudomonas syringae; Carbohydrates; Antibiotics; Sequence motif analysis

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Medicine


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

Added On: 23/03/2014 10:19

Documents:
journal.ppat.1003898.pdf

Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Structural biology Biophysics Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)