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O serotype-independent susceptibility of Pseudomonas aeruginosa to lectin-like pyocins.

Ghequire MG, Dingemans J, Pirnay JP, De Vos D, Cornelis P, De Mot R - Microbiologyopen (2014)

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.

View Article: PubMed Central - PubMed

Affiliation: Centre of Microbial and Plant Genetics, University of Leuven, 3001, Heverlee, Belgium.

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Structural diversity of L pyocins. (A) Cartoon representation of PyoL1 from Pseudomonas aeruginosa C1433 (PDB 4LE7). (B) Structural model of PyoL2 from strain 62. Estimated accuracy of the model is 1.42 (C-score) with a template modeling score of 0.91 ± 0.06 and root mean square deviation of 3.0 ± 2.2 Å. (C) Cartoon-surface representations of the PyoL2 model. Residues constituting the D-rhamnose binding sites IIIC and IIC are shown as blue and red spheres, respectively. Nonconserved residues differing between PyoL2 and PyoL1 are indicated in black. Conservative substitutions are not marked: V-M, E-Q, G-A, I-L, I-V, A-V, R-K, N-D, T-S.
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fig05: Structural diversity of L pyocins. (A) Cartoon representation of PyoL1 from Pseudomonas aeruginosa C1433 (PDB 4LE7). (B) Structural model of PyoL2 from strain 62. Estimated accuracy of the model is 1.42 (C-score) with a template modeling score of 0.91 ± 0.06 and root mean square deviation of 3.0 ± 2.2 Å. (C) Cartoon-surface representations of the PyoL2 model. Residues constituting the D-rhamnose binding sites IIIC and IIC are shown as blue and red spheres, respectively. Nonconserved residues differing between PyoL2 and PyoL1 are indicated in black. Conservative substitutions are not marked: V-M, E-Q, G-A, I-L, I-V, A-V, R-K, N-D, T-S.

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.


O serotype-independent susceptibility of Pseudomonas aeruginosa to lectin-like pyocins.

Ghequire MG, Dingemans J, Pirnay JP, De Vos D, Cornelis P, De Mot R - Microbiologyopen (2014)

Structural diversity of L pyocins. (A) Cartoon representation of PyoL1 from Pseudomonas aeruginosa C1433 (PDB 4LE7). (B) Structural model of PyoL2 from strain 62. Estimated accuracy of the model is 1.42 (C-score) with a template modeling score of 0.91 ± 0.06 and root mean square deviation of 3.0 ± 2.2 Å. (C) Cartoon-surface representations of the PyoL2 model. Residues constituting the D-rhamnose binding sites IIIC and IIC are shown as blue and red spheres, respectively. Nonconserved residues differing between PyoL2 and PyoL1 are indicated in black. Conservative substitutions are not marked: V-M, E-Q, G-A, I-L, I-V, A-V, R-K, N-D, T-S.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4263511&req=5

fig05: Structural diversity of L pyocins. (A) Cartoon representation of PyoL1 from Pseudomonas aeruginosa C1433 (PDB 4LE7). (B) Structural model of PyoL2 from strain 62. Estimated accuracy of the model is 1.42 (C-score) with a template modeling score of 0.91 ± 0.06 and root mean square deviation of 3.0 ± 2.2 Å. (C) Cartoon-surface representations of the PyoL2 model. Residues constituting the D-rhamnose binding sites IIIC and IIC are shown as blue and red spheres, respectively. Nonconserved residues differing between PyoL2 and PyoL1 are indicated in black. Conservative substitutions are not marked: V-M, E-Q, G-A, I-L, I-V, A-V, R-K, N-D, T-S.
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.

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.

View Article: PubMed Central - PubMed

Affiliation: Centre of Microbial and Plant Genetics, University of Leuven, 3001, Heverlee, Belgium.

Show MeSH
Related in: MedlinePlus