O serotype-independent susceptibility of Pseudomonas aeruginosa to lectin-like pyocins.
Bottom Line: The recombinant proteins exhibit species-specific antagonistic activities down to nanomolar concentrations against clinical and environmental P. aeruginosa strains, including several multidrug-resistant isolates.No correlation was found between L pyocin susceptibility and phylogenetic relatedness of P. aeruginosa isolates.Sensitive strains were retrieved in 13 out of 15 O serotypes tested, excluding the possibility that the highly variable and immunogenic O serotype antigen of the LPS coating would represent a dominant susceptibility-discriminating factor.
Affiliation: Centre of Microbial and Plant Genetics, University of Leuven, 3001, Heverlee, Belgium.Show MeSH
Related in: MedlinePlus
Mentions: The pronounced sequence homology between PyoL1 and PyoL2 (86% amino acid identity) enabled to generate a reliable model for PyoL2 (Fig. 5B) based on the PyoL1 structure (Fig. 5A) (McCaughey et al. 2014). Nonconservative amino acid substitutions between the PyoL1 and PyoL2 sequences predominantly cluster on one side of the amino-terminal MMBL domain (Fig. 5C). These patches on PyoL1 and PyoL2 are good candidate interaction sites mediating differential activity toward susceptible strains.
Affiliation: Centre of Microbial and Plant Genetics, University of Leuven, 3001, Heverlee, Belgium.