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Applied and Environmental Microbiology, February 2000, p. 487-492, Vol. 66, No. 2
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Quinolobactin, a New Siderophore of Pseudomonas fluorescens ATCC 17400, the Production of Which Is Repressed by the Cognate Pyoverdine

Dimitris Mossialos,1,2 Jean-Marie Meyer,3 Herbert Budzikiewicz,4 Ulrich Wolff,4 Nico Koedam,2 Christine Baysse,1,2 Vanamala Anjaiah,1,2 and Pierre Cornelis1,2,*

Department of Immunology, Parasitology, and Ultrastructure, Flanders Interuniversity Institute for Biotechnology,1 and Laboratory of Microbial Interactions, Vrije Universiteit Brussel,2 Sint Genesius Rode, Belgium; Laboratoire de Microbiologie et de Génétique, U.P.R.S.A., Centre National de la Recherche Scientifique, Université Louis Pasteur, Strasbourg, France3; and Institüt für Organische Chemie der Universität zu Köln, Cologne, Germany4

Received 24 May 1999/Accepted 10 October 1999

Transposon mutant strain 3G6 of Pseudomonas fluorescens ATCC 17400 which was deficient in pyoverdine production, was found to produce another iron-chelating molecule; this molecule was identified as 8-hydroxy-4-methoxy-quinaldic acid (designated quinolobactin). The pyoverdine-deficient mutant produced a supplementary 75-kDa iron-repressed outer membrane protein (IROMP) in addition to the 85-kDa IROMP present in the wild type. The mutant was also characterized by substantially increased uptake of 59Fe-quinolobactin. The 75-kDa IROMP was produced by the wild type after induction by quinolobactin-containing culture supernatants obtained from the pyoverdine-negative mutant or by purified quinolobactin. Conversely, adding purified wild-type pyoverdine to the growth medium resulted in suppression of the 75-kDa IROMP in the pyoverdine-deficient mutant; however, suppression was not observed when Pseudomonas aeruginosa PAO1 pyoverdine, a siderophore utilized by strain 3G6, was added to the culture. Therefore, we assume that the quinolobactin receptor is the 75-kDa IROMP and that the quinolobactin-mediated iron uptake system is repressed by the cognate pyoverdine.

* Corresponding author. Mailing address: Department of Immunology, Parasitology, and Ultrastructure, Flanders Interuniversity Institute for Biotechnology, Paardenstraat 65, B-1640 Sint Genesius Rode, Belgium. Phone: 32 2 3590221. Fax: 32 2 3590390. E-mail: pcornel{at}vub.ac.be.

Applied and Environmental Microbiology, February 2000, p. 487-492, Vol. 66, No. 2
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Godert, A. M., Jin, M., McLafferty, F. W., Begley, T. P. (2007). Biosynthesis of the Thioquinolobactin Siderophore: an Interesting Variation on Sulfur Transfer. J. Bacteriol. 189: 2941-2944 [Abstract] [Full Text]  
  • Baysse, C., Matthijs, S., Schobert, M., Layer, G., Jahn, D., Cornelis, P. (2003). Co-ordination of iron acquisition, iron porphyrin chelation and iron-protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens. Microbiology 149: 3543-3552 [Abstract] [Full Text]  
  • de Chial, M., Ghysels, B., Beatson, S. A., Geoffroy, V., Meyer, J. M., Pattery, T., Baysse, C., Chablain, P., Parsons, Y. N., Winstanley, C., Cordwell, S. J., Cornelis, P. (2003). Identification of type II and type III pyoverdine receptors from Pseudomonas aeruginosa. Microbiology 149: 821-831 [Abstract] [Full Text]  


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