Lectin-like bacteriocins from pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor

Laura C McCaughey, Rhys Grinter, Inokentijs Josts, Aleksander W Roszak, Kai I Waløen, Richard J Cogdell, Joel Milner, Tom Evans, Sharon Kelly, Nicholas P Tucker, Olwyn Byron, Brian Smith, Daniel Walker

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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.
Original languageEnglish
Article numbere1003898
Number of pages15
JournalPLOS Pathogens
Issue number2
Publication statusPublished - 6 Feb 2014


  • cellular receptor
  • lectin-like bacteriocins
  • pseudomonas spp
  • D-rhamnose
  • lipopolysaccharide

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