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Ferric-Pyoverdine Recognition by Fpv Outer Membrane Proteins of Pseudomonas protegens Pf-5

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https://ir.library.oregonstate.edu/concern/articles/2f75r8676

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  • The soil bacterium Pseudomonas protegens Pf-5 (previously called P. fluorescens Pf-5) produces two siderophores, enantio-pyochelin and a compound in the large and diverse pyoverdine family. Using high-resolution mass spectroscopy, we determined the structure of the pyoverdine produced by Pf-5. In addition to producing its own siderophores, Pf-5 also utilizes ferric complexes of some pyoverdines produced by other strains of Pseudomonas spp. as sources of iron. Previously, phylogenetic analysis of the 45 TonB-dependent outer membrane proteins in Pf-5 indicated that six are in a well-supported clade with ferric-pyoverdine receptors (Fpvs) from other Pseudomonas spp. We used a combination of phylogenetics, bioinformatics, mutagenesis, pyoverdine structural determinations, and cross-feeding bioassays to assign specific ferric-pyoverdine substrates to each of the six Fpvs of Pf-5. We identified at least one ferric-pyoverdine that was taken up by each of the six Fpvs of Pf-5. Functional redundancy of the Pf-5 Fpvs was also apparent, with some ferric-pyoverdines taken up by all mutants with a single Fpv deletion but not by a mutant having deletions in two of the Fpv-encoding genes. Finally, we demonstrated that phylogenetically related Fpvs take up ferric complexes of structurally related pyoverdines, thereby establishing structure-function relationships that can be employed in the future to predict the pyoverdine substrates of Fpvs in other Pseudomonas spp.
  • Keywords: Bacterial siderophores, Swiss model workspace, Putida WC358, Nonribosomal peptide synthetases, Nucleotide sequence analysis, Fluorescent pseudomonas, Ferripyoverdine redceptor, Heterologous siderophores, Nonfluorescent pseudomonas, Pseudobactin receptor
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  • Hartney, S. L., Mazurier, S., Girard, M. K., Mehnaz, S., Davis, 2., Edward W, Gross, H., . . . Loper, J. E. (2013). Ferric-pyoverdine recognition by fpv outer membrane proteins of pseudomonas protegens pf-5. Journal of Bacteriology, 195(4), 765-776. doi:10.1128/JB.01639-12
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  • 195
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  • 4
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  • H. Gross and S. Mehnaz gratefully acknowledge the generous contribution of the Alexander von Humboldt Foundation, which provided financial support (Georg Forster Fellowship awarded to S. Mehnaz). This work was supported by grants 2006-35319-17427 and 2008-35600-18770 from the USDA National Institute of Food and Agriculture.
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