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Journal of Bacteriology, October 2008, p. 6548-6558, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00784-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Metal Dependence of Pyoverdine Interactions with Its Outer Membrane Receptor FpvA{triangledown}

Jason Greenwald,1* Gabrielle Zeder-Lutz,2 Agnès Hagege,3 Hervé Celia,1 and Franc Pattus1

Département Récepteurs et Protéines Membranaires,1 Département Biotechnologie des Interactions Macromoléculaires, Institut Gilbert-Laustriat, UMR 7175-LC1 CNRS, ESBS, Blvd. Sébastien Brant, F-67413 Illkirch, Strasbourg, France,2 Laboratoire de Chimie Analytique et Sciences Séparatives, IPHC-DSA (UMR7178) ECPM, 25 rue Becquerel, 67087 Strasbourg, France3

Received 4 June 2008/ Accepted 7 July 2008

To acquire iron, Pseudomonas aeruginosa secretes the fluorescent siderophore pyoverdine (Pvd), which chelates iron and shuttles it into the cells via the specific outer membrane transporter FpvA. We studied the role of iron and other metals in the binding and transport of Pvd by FpvA and conclude that there is no significant affinity between FpvA and metal-free Pvd. We found that the fluorescent in vivo complex of iron-free FpvA-Pvd is in fact a complex with aluminum (FpvA-Pvd-Al) formed from trace aluminum in the growth medium. When Pseudomonas aeruginosa was cultured in a medium that had been treated with a metal affinity resin, the in vivo formation of the FpvA-Pvd complex and the recycling of Pvd on FpvA were nearly abolished. The accumulation of Pvd in the periplasm of Pseudomonas aeruginosa was also reduced in the treated growth medium, while the addition of 1 µM AlCl3 to the treated medium restored the effects of trace metals observed in standard growth medium. Using fluorescent resonance energy transfer and surface plasmon resonance techniques, the in vitro interactions between Pvd and detergent-solubilized FpvA were also shown to be metal dependent. We demonstrated that FpvA binds Pvd-Fe but not Pvd and that Pvd did not compete with Pvd-Fe for FpvA binding. In light of our finding that the Pvd-Al complex is transported across the outer membrane of Pseudomonas aeruginosa, a model for siderophore recognition based on a metal-induced conformation followed by redox selectivity for iron is discussed.

* Corresponding author. Mailing address: Laboratorium für Physikalische Chemie, ETH Zürich, Zürich, Switzerland. Phone: 41(0)446334924. Fax: 41(0)446321021. E-mail: jason.greenwald{at}phys.chem.ethz.ch

{triangledown} Published ahead of print on 18 July 2008.

Journal of Bacteriology, October 2008, p. 6548-6558, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00784-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Shirley, M., Lamont, I. L. (2009). Role of TonB1 in Pyoverdine-Mediated Signaling in Pseudomonas aeruginosa. J. Bacteriol. 191: 5634-5640 [Abstract] [Full Text]  
  • Cornelis, P. (2008). Unexpected Interaction of a Siderophore with Aluminum and Its Receptor. J. Bacteriol. 190: 6541-6543 [Full Text]  


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