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Updated: Aug 28, 2026

High-throughput Siderophore Screening from Environmental Samples: Plant Tissues, Bulk Soils, and Rhizosphere Soils
Published on: February 9, 2019
Outer membrane protein mediating iron uptake via pyoverdinpss, the fluorescent siderophore produced by Pseudomonas
Abstract:
In an iron-limited environment Pseudomonas syringae pv. syringae B301D produces a yellow-green fluorescent siderophore called pyoverdinpss which functions in high-affinity iron transport. Two-dimensional electrophoretic comparisons of the outer membrane proteins of strain B301D identified nine proteins which were expressed at low (50 nM) but not at high (10 microM) iron concentrations. Except for the minor protein 8e, the iron-regulated proteins exhibited high molecular weights ranging from approximately 74,000 to 80,000. A mutant of strain B301D incapable of iron uptake (Iu-) from ferric pyoverdinpss lacked the 74,000-molecular-weight protein 4a, which was the major iron-regulated outer membrane protein. In contrast, a nonfluorescent mutant (Flu-) unable to synthesize pyoverdinpss showed no quantitative or qualitative difference in its outer membrane profile from that of the wild-type strain. In plant pathogenicity tests the Iu- and Flu- strains caused typical brown necrotic and sunken lesions in immature sweet cherry fruit which were indistinguishable from those of the wild-type strain. Thus, excretion of pyoverdinpss and subsequent Fe(III) uptake do not have a determinative role in the pathogenicity or virulence of P. syringae pv. syringae.
Insights
Pseudomonas syringae pv. syringae produces pyoverdine (a siderophore) for iron transport. Iron uptake via pyoverdine is not essential for this bacterium
Area of Science:
- Microbiology
- Plant Pathology
- Biochemistry
Background:
- Pseudomonas syringae pv. syringae B301D produces pyoverdine, a fluorescent siderophore, for high-affinity iron transport in iron-limited conditions.
- Iron uptake is crucial for bacterial growth and virulence, often mediated by specific outer membrane proteins.
Purpose of the Study:
- To investigate the role of pyoverdine and iron uptake in the pathogenicity of Pseudomonas syringae pv. syringae.
- To identify iron-regulated outer membrane proteins involved in iron transport.
Main Methods:
- Two-dimensional electrophoresis was used to compare outer membrane proteins between low and high iron conditions.
- Mutants deficient in iron uptake (Iu-) or pyoverdine synthesis (Flu-) were created and analyzed.
- Pathogenicity tests were conducted on immature sweet cherry fruit.
Main Results:
- Nine iron-regulated outer membrane proteins were identified, mostly with high molecular weights (74,000-80,000 Da).
- The iron uptake mutant (Iu-) lacked a major 74,000 Da iron-regulated protein (protein 4a).
- The nonfluorescent mutant (Flu-) showed no difference in outer membrane protein profiles compared to the wild-type.
Conclusions:
- Pyoverdine production and subsequent iron(III) uptake are not critical for the pathogenicity or virulence of Pseudomonas syringae pv. syringae on cherry fruit.
- Specific outer membrane proteins are regulated by iron availability, suggesting a role in iron transport, but this process is not essential for virulence in this context.
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