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J. Biol. Chem., Vol. 280, Issue 21, 20222-20230, May 27, 2005

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Binding of Iron-free Siderophore, a Common Feature of Siderophore Outer Membrane Transporters of Escherichia coli and Pseudomonas aeruginosa^*

Françoise Hoegy, Hervé Celia, Gaëtan L. Mislin, Michel Vincent, Jacques Gallay, and Isabelle J. Schalk¶

From the Département des Récepteurs et Protéines Membranaires, UPR 9050 CNRS, ESBS, Bld. Sébastien Brant, F-67413 Illkirch, Strasbourg and IBBMC UMR CNRS 8619, Btiment 430, Université Paris-Sud, 91405 Orsay Cedex, France

TonB-dependent iron transporters present in the outer membranes of Gram-negative bacteria transport ferric-siderophore complexes into the periplasm. This requires proton motive force and an integral inner membrane complex, TonB-ExbB-ExbD. Recognition of iron-free siderophores by TonB-dependent outer membrane transporters (OMT) has only been described for a subfamily called OMT_N. These OMT_Ns have an additional domain at the N terminus, which interacts with an inner membrane regulatory protein to activate a cytoplasmic factor. This induces transcription of iron transport genes. Here we showed that the ability to bind aposiderophores is not specific to the OMT_N subfamily but may be a more general feature of OMTs. FhuA, the ferrichrome OMT in Escherichia coli, and FptA, the pyochelin (Pch) OMT in Pseudomonas aeruginosa, were both able to bind in vitro and in vivo the apo-forms and the ferric forms of their corresponding siderophore at a common binding site. FptA produced in P. aeruginosa cells grown in an iron-deficient medium copurifies with a ligand that, as characterized by fluorescence, is iron-free Pch. As described previously for the FpvA transporter (pyoverdine OMT in P. aeruginosa), it appears that in conditions of iron limitation all the FptA receptors at the cell surface are loaded with apoPch. This FptA-Pch complex is less stable in vitro than the previously described copurified FpvA-Pvd complex and can be loaded with iron in vitro in the presence of Pch-Fe, citrate-Fe, or ferrichrome-Fe. These findings improved our understanding of the iron uptake mechanism via siderophores in Gram-negative bacteria.

Received for publication, January 21, 2005 , and in revised form, February 24, 2005.

^* This work was supported by Vaincre la Mucoviscidose and by the CNRS. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dépt. des Récepteurs et Protéines Membranaires, UPR 9050 CNRS, ESBS, Bld. Sébastien Brant, BP 10412, F-67413 Illkirch, Strasbourg, France. Tel.: 33-3-90-24-47-19; Fax: 33-3-90-24-48-29; E-mail: schalk{at}esbs.u-strasbg.fr.

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