Lectin-Like Bacteriocins from Pseudomonas spp. Utilise D-Rhamnose Containing Lipopolysaccharide as a Cellular Receptor

PLoS Pathogens

Rhys Grinter¹  Richard J. Cogdell¹  Nicholas P. Tucker¹  Inokentijs Josts¹  Laura C. McCaughey¹  Sharon Kelly²  Olwyn Byron²  Tom Evans²  Kai I. Waløen²  Joel Milner³  Daniel Walker³  Brian Smith⁴  Aleksander W. Roszak⁵ 

[1] Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom;Institute of Molecular Cell and Systems Biology, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow, United Kingdom;School of Life Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom;Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde, Glasgow, United Kingdom;WestCHEM, School of Chemistry, College of Science and Engineering, University of Glasgow, Glasgow, United Kingdom

关键词: Bacteriocins;    Lectins;    Pseudomonas aeruginosa;    Polysaccharides;    Pseudomonas syringae;    Sequence motif analysis;    Antibiotics;    Carbohydrates;   

DOI  :  10.1371/journal.ppat.1003898

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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.

【 授权许可】

CC BY