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Applied and Environmental Microbiology, April 2001, p. 1718-1727, Vol. 67, No. 4
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.4.1718-1727.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of Fluorescent and Nonfluorescent Peptide Siderophores Produced by Pseudomonas syringae Strains and Their Potential Use in Strain Identification

Alain Bultreys,1,* Isabelle Gheysen,1 Henri Maraite,2 and Edmond de Hoffmann3

Département de Biotechnologie, Centre de Recherches Agronomiques de Gembloux, Ministère des Classes Moyennes et de l'Agriculture, B-5030 Gembloux,1 and Unité de Phytopathologie2 and Laboratoire de Spectrométrie de Masse,3 Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium

Received 5 September 2000/Accepted 31 January 2001

Nonfluorescent highly virulent strains of Pseudomonas syringae pv. aptata isolated in different European countries and in Uruguay produce a nonfluorescent peptide siderophore, the production of which is iron repressed and specific to these strains. The amino acid composition of this siderophore is identical to that of the dominant fluorescent peptide siderophore produced by fluorescent P. syringae strains, and the molecular masses of the respective Fe(III) chelates are 1,177 and 1,175 atomic mass units. The unchelated nonfluorescent siderophore is converted into the fluorescent siderophore at pH 10, and colors and spectral characteristics of the unchelated siderophores and of the Fe(III)-chelates in acidic conditions are similar to those of dihydropyoverdins and pyoverdins, respectively. The nonfluorescent siderophore is used by fluorescent and nonfluorescent P. syringae strains. These results and additional mass spectrometry data strongly suggest the presence of a pyoverdin chromophore in the fluorescent siderophore and a dihydropyoverdin chromophore in the nonfluorescent siderophore, which are both ligated to a succinamide residue. When chelated, the siderophores behave differently from typical pyoverdins and dihydropyoverdins in neutral and alkaline conditions, apparently because of the ionization occurring around pH 4.5 of carboxylic acids present in beta -hydroxyaspartic acid residues of the peptide chains. These differences can be detected visually by pH-dependent changes of the chelate colors and spectrophotochemically. These characteristics and the electrophoretic behavior of the unchelated and chelated siderophores offer new tools to discriminate between saprophytic fluorescent Pseudomonas species and fluorescent P. syringae and P. viridiflava strains and to distinguish between the two siderovars in P. syringae pv. aptata.

* Corresponding author. Mailing address: Département de Biotechnologie, Centre de Recherches Agronomiques de Gembloux, 234 Chaussée de Charleroi, B-5030 Gembloux, Belgium. Phone: (32) 81 62 73 88. Fax: (32) 81 62 73 99. E-mail: bultreys{at}cragx.fgov.be.

Applied and Environmental Microbiology, April 2001, p. 1718-1727, Vol. 67, No. 4
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.4.1718-1727.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.