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_name
PLoS Pathogjournal_title
PLoS pathogensauthors
McCaughey LC,Grinter R,Josts I,Roszak AW,Waløen KI,Cogdell RJ,Milner J,Evans T,Kelly S,Tucker NP,Byron O,Smith B,Walker Ddoi
10.1371/journal.ppat.1003898subject
Has Abstractpub_date
2014-02-06 00:00:00pages
e1003898issue
2eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-13-01910journal_volume
10pub_type
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