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

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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.

ORCID iDs

McCaughey, Laura C, Grinter, Rhys, Josts, Inokentijs, Roszak, Aleksander W, Waløen, Kai I, Cogdell, Richard J, Milner, Joel, Evans, Tom, Kelly, Sharon, Tucker, Nicholas P ORCID logoORCID: https://orcid.org/0000-0002-6331-3704, Byron, Olwyn, Smith, Brian and Walker, Daniel ORCID logoORCID: https://orcid.org/0000-0002-4206-2942;
CORE (COnnecting REpositories)