The Structure of the Pyoverdin Isolated from Various Pseudomonas syringae Pathovars

Jülich, Markus; Taraz, K.; Budzikiewicz, H.; Geoffroy, Valérie; Meyer, Jean‐Marie; Gardan, Louis

doi:10.1515/znc-2001-9-1003

Cited by 25 publications

(16 citation statements)

References 5 publications

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“…syringae 22d/93. It has been known for a long time that plant-associated P. syringae isolates produce pyoverdin, a peptide-type siderophore that causes the green fluorescence responsible for the term "fluorescent pseudomonads" (7,9,25). However, the hypoth- esis that one bacterial isolate produces one type of siderophore has been revised due to the increased availability of genome sequence information so that it is now acknowledged that there is great redundancy in iron uptake systems, which includes the presence of multiple of siderophore receptors in, and the production of several different siderophores by, a single bacterium (18).…”

Section: Discussionmentioning

confidence: 99%

Impact of Siderophore Production by Pseudomonas syringae pv. syringae 22d/93 on Epiphytic Fitness and Biocontrol Activity against Pseudomonas syringae pv. glycinea 1a/96

Wensing

Braun

Büttner

et al. 2010

Appl Environ Microbiol

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The use of naturally occurring microbial antagonists to suppress plant diseases offers a favorable alternative to classical methods of plant protection. The soybean epiphyte Pseudomonas syringae pv. syringae strain 22d/93 shows great potential for controlling P. syringae pv. glycinea, the causal agent of bacterial blight of soybean. Its activity against P. syringae pv. glycinea is highly reproducible even in field trials, and the suppression mechanisms involved are of special interest. In this work we demonstrated that P. syringae pv. syringae 22d/93 produced a significantly larger amount of siderophores than the pathogen P. syringae pv. glycinea produced. While P. syringae pv. syringae 22d/93 and P. syringae pv. glycinea produce the same siderophores, achromobactin and pyoverdin, the regulation of siderophore biosynthesis in the former organism is very different from that in the latter organism. The epiphytic fitness of P. syringae pv. syringae 22d/93 mutants defective in siderophore biosynthesis was determined following spray inoculation of soybean leaves. The population size of the siderophore-negative mutant P. syringae pv. syringae strain 22d/93⌬Sid was 2 orders of magnitude lower than that of the wild type 10 days after inoculation. The growth deficiency was compensated for when wound inoculation was used, indicating the availability of iron in the presence of small lesions on the leaves. Our results suggest that siderophore production has an indirect effect on the biocontrol activity of P. syringae pv. syringae 22d/93. Although siderophore-defective mutants of P. syringae pv. syringae 22d/93 still suppressed development of bacterial blight caused by P. syringae pv. glycinea, siderophore production enhanced the epiphytic fitness and thus the competitiveness of the antagonist.Application of epiphytic bacteria as control agents is considered a nonpolluting approach for alternative plant protection, and a number of potential antagonistic isolates have been described. However, only a few of these isolates have proven to be as effective under field conditions as they are in laboratory setups (1, 39). It has been proposed that several attributes contribute to biocontrol, including competition for nutrients, antibiosis, niche exclusion, and interference with cell signaling systems (13, 36).Many potential antagonists have been selected from the fluorescent pseudomonad group, as this group includes various nonpathogenic species that are adapted to plant colonization and well known for their competitiveness (11,19,20). Pseudomonas fluorescens CHA0 has been proposed as biocontrol organism that can be used against several soilborne plant diseases (13). It has been suggested that secondary metabolites, such as 2,4-diacetylphloroglucinol, hydrogen cyanide, pyoverdin, and salicylate, are active principles in this isolate (11,13).P. fluorescens Pf-5 is a rhizosphere bacterium that suppresses seedling emergence diseases and produces a spectrum of antibiotics toxic to plant-pathogenic fungi (34). Pseudomonas putida WCS358, ...

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Section: Discussionmentioning

confidence: 99%

Impact of Siderophore Production by Pseudomonas syringae pv. syringae 22d/93 on Epiphytic Fitness and Biocontrol Activity against Pseudomonas syringae pv. glycinea 1a/96

Wensing

Braun

Büttner

et al. 2010

Appl Environ Microbiol

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“…It was superior to the generally used IEF technique (1,19,22,27,28) in three ways: it enabled the detection of lower pyoverdin production, such as that in P. ficuserectae; it enabled the distinction of typical pyoverdins from atypical pyoverdins (Fig. 1); and it was more reliable.…”

Section: Discussionmentioning

confidence: 98%

“…3). Fe(III) incorporation experiments are often carried out to confirm the results of IEF analyses (1,19,27,28). However, the same membrane receptor can incorporate different pyoverdins if they have some similarities (2,31,33,39), and bacteria can possess additional membrane receptors to incorporate heterogeneous pyoverdins (11,23).…”

Section: Discussionmentioning

confidence: 99%

“…More than 40 pyoverdin peptide chain compositions have been identified in the group containing the arginine dihydrolase-positive, saprophytic or opportunistic animal-pathogenic, fluorescent Pseudomonas species (14), but only one composition has been found in the group containing the arginine dihydrolase-negative, phytopathogenic, fluorescent Pseudomonas species (7,8,10,19). The latter group includes Pseudomonas syringae, Pseudomonas viridiflava, and Pseudomonas cichorii (29).…”

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confidence: 99%

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High-Performance Liquid Chromatography Analyses of Pyoverdin Siderophores Differentiate among Phytopathogenic Fluorescent Pseudomonas Species

Bultreys¹,

Gheysen²,

Wathelet

et al. 2003

Appl Environ Microbiol

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The relationship of pyoverdins produced by 41 pathovars of Pseudomonas syringae and by phytopathogenic Pseudomonas species was investigated. A high-performance liquid chromatography method for analyzing the culture medium proved to be superior to isoelectric focusing for detecting pyoverdin production, for differentiating slightly different pyoverdins, and for differentiating atypical from typical Fe(III)-chelated pyoverdins. Nonfluorescent strains were found in Pseudomonas amygdali, Pseudomonas meliae, Pseudomonas fuscovaginae, and P. syringae. Pseudomonas agarici and Pseudomonas marginalis produced typical pyoverdins. Among the arginine dihydrolase-negative fluorescent Pseudomonas species, spectral, amino acid, and mass spectrometry analyses underscored for the first time the clear similarities among the pyoverdins produced by related species. Within this group, the oxidase-negative species Pseudomonas viridiflava and Pseudomonas ficuserectae and the pathovars of P. syringae produced the same atypical pyoverdin, whereas the oxidase-positive species Pseudomonas cichorii produced a similar atypical pyoverdin that contained a glycine instead of a serine. The more distantly related species Pseudomonas asplenii and Pseudomonas fuscovaginae both produced a less similar atypical pyoverdin. The spectral characteristics of Fe(III)-chelated atypical pyoverdins at pH 7.0 were related to the presence of two ␤-hydroxyaspartic acids as iron ligands, whereas in typical pyoverdins one of the ligands is always ornithine based. The peptide chain influenced the chelation of iron more in atypical pyoverdins. Our results demonstrated that there is relative pyoverdin conservation in the amino acids involved in iron chelation and that there is faster evolution of the other amino acids, highlighting the usefulness of pyoverdins in systematics and in identification.

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“…Pyoverdine production by P. aeruginosa pvdH::Gm r and asd::Gm r mutants was assessed by growing the mutants in iron-limiting Casamino Acids (CAA) broth (17). The same mutants were also grown in CAA broth supplemented with 1.5 mM L-2,4-diaminobutyrate.…”

Section: Methodsmentioning

confidence: 99%

Functional Characterization of an Aminotransferase Required for Pyoverdine Siderophore Biosynthesis in Pseudomonas aeruginosa PAO1

2004

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The fluorescent dihydroxyquinoline chromophore of the pyoverdine siderophore in Pseudomonas is a condensation product of D-tyrosine and L-2,4-diaminobutyrate. Both pvdH and asd (encoding aspartate ␤-semialdehyde dehydrogenase) knockout mutants of Pseudomonas aeruginosa PAO1 were unable to synthesize pyoverdine under iron-limiting conditions in the absence of L-2,4-diaminobutyrate in the culture media. The pvdH gene was subcloned, and the gene product was hyperexpressed and purified from P. aeruginosa PAO1. PvdH was found to catalyze an aminotransferase reaction, interconverting aspartate ␤-semialdehyde and L-2,4-diaminobutyrate. Steady-state kinetic analysis with a novel coupled assay established that the enzyme adopts a ping-pong kinetic mechanism and has the highest specificity for ␣-ketoglutarate. The specificity of the enzyme toward the smaller keto acid pyruvate is 41-fold lower. The enzyme has negligible activity toward other keto acids tested. Homologues of PvdH were present in the genomes of other Pseudomonas spp. These homologues were found in the DNA loci of the corresponding genomes that contain other pyoverdine synthesis genes. This suggests that there is a general mechanism of L-2,4-diaminobutyrate synthesis in Pseudomonas strains that produce the pyoverdine siderophore.

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The Structure of the Pyoverdin Isolated from Various Pseudomonas syringae Pathovars

Cited by 25 publications

References 5 publications

Impact of Siderophore Production by Pseudomonas syringae pv. syringae 22d/93 on Epiphytic Fitness and Biocontrol Activity against Pseudomonas syringae pv. glycinea 1a/96

Impact of Siderophore Production by Pseudomonas syringae pv. syringae 22d/93 on Epiphytic Fitness and Biocontrol Activity against Pseudomonas syringae pv. glycinea 1a/96

High-Performance Liquid Chromatography Analyses of Pyoverdin Siderophores Differentiate among Phytopathogenic Fluorescent Pseudomonas Species

Functional Characterization of an Aminotransferase Required for Pyoverdine Siderophore Biosynthesis in Pseudomonas aeruginosa PAO1

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