Lectin-like bacteriocins from pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor
McCaughey, Laura C and Grinter, Rhys and Josts, Inokentijs and Roszak, Aleksander W and Waløen, Kai I and Cogdell, Richard J and Milner, Joel and Evans, Tom and Kelly, Sharon and Tucker, Nicholas P and Byron, Olwyn and Smith, Brian and Walker, Daniel (2014) Lectin-like bacteriocins from pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. PLOS Pathogens, 10 (2). e1003898. ISSN 1553-7366 (https://doi.org/10.1371/journal.ppat.1003898)
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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.
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Item type: Article ID code: 47220 Dates: DateEvent6 February 2014Published10 December 2013AcceptedSubjects: Medicine > Pharmacy and materia medica Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Depositing user: Pure Administrator Date deposited: 18 Mar 2014 10:20 Last modified: 07 Aug 2024 01:13 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/47220