Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor.
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 polysacchari...
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2014
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oai:doaj.org-article:8c5d476138b54187bf9cc442c4860eed2021-11-18T06:07:02ZLectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor.1553-73661553-737410.1371/journal.ppat.1003898https://doaj.org/article/8c5d476138b54187bf9cc442c4860eed2014-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24516380/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Lectin-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.Laura C McCaugheyRhys GrinterInokentijs JostsAleksander W RoszakKai I WaløenRichard J CogdellJoel MilnerTom EvansSharon KellyNicholas P TuckerOlwyn ByronBrian SmithDaniel WalkerPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 10, Iss 2, p e1003898 (2014) |
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DOAJ |
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DOAJ |
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EN |
| topic |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 |
| spellingShingle |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 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 Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| description |
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. |
| format |
article |
| author |
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 |
| author_facet |
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 |
| author_sort |
Laura C McCaughey |
| title |
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| title_short |
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| title_full |
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| title_fullStr |
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| title_full_unstemmed |
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor. |
| title_sort |
lectin-like bacteriocins from pseudomonas spp. utilise d-rhamnose containing lipopolysaccharide as a cellular receptor. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2014 |
| url |
https://doaj.org/article/8c5d476138b54187bf9cc442c4860eed |
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