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Copurification of the FpvA Ferric Pyoverdin Receptor of Pseudomonas aeruginosa with Its Iron-Free Ligand:  Implications for Siderophore-Mediated Iron Transport

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    Copurification of the FpvA Ferric Pyoverdin Receptor of Pseudomonasaeruginosa with Its Iron-Free Ligand:  Implications for Siderophore-Mediated Iron Transport†
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    Département des Récepteurs et Protéines Membranaires, UPR 9050 CNRS, ESBS, Bld Sébastien Brant, F-67 400 Illkirch, Strasbourg, France, Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídenská 1083, 142 20 Prague 4, Czech Republic, Signaux Biologiques et Spectrométrie de Masse, Institut de Pharmacologie et de Biologie Structurale, 31 077 Toulouse Cedex, France, Laboratoire de Spectrométrie de Masse Bio-organique, associé au CNRS, Faculté de Chimie, 1 rue Blaise Pascal, 67 008 Strasbourg Cedex, France, and Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6
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    Biochemistry

    Cite this: Biochemistry 1999, 38, 29, 9357–9365
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    https://doi.org/10.1021/bi990421x
    Published June 30, 1999
    Copyright © 1999 American Chemical Society
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    Abstract

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    The Pseudomonasaeruginosa FpvA receptor is a TonB-dependent outer membrane transport protein that catalyzes uptake of ferric pyoverdin across the outer membrane. Surprisingly, FpvA expressed in P. aeruginosa grown in an iron-deficient medium copurifies with a ligand X that we have characterized by UV, fluorescence, and mass spectrometry as being iron-free pyoverdin (apo-PaA). PaA was absent from FpvA purified from a PaA−deficient P. aeruginosa strain. The properties of ligand binding in vitro revealed very similar affinities of apo-PaA and ferric−PaA to FpvA. Fluorescence resonance energy transfer was used to study in vitro the formation of the FpvA−PaA−Fe complex in the presence of PaA−Fe or citrate−Fe. The circular dichroism spectrum of FpvA indicated a 57% β-structure content typical of porins and in agreement with the 3D structures of the siderophore receptors FhuA and FepA. In the absence of the protease's inhibitors, a truncated form of FpvA lacking 87 amino acids at its N-terminus was purified. This truncated form still bound PaA, and its β-sheet content was conserved. This N-terminal region displays significant homology to the N-terminal periplasmic extensions of FecA from Escherichia coli and PupB from Pseudomonas putida, which were previously shown to be involved in signal transduction. This suggests a similar function for FpvA. The mechanism of iron transport in P. aeruginosa via the pyoverdin pathway is discussed in the light of all these new findings.

    Copyright © 1999 American Chemical Society

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    †

     This work was funded by the Centre National de la Recherche Scientifique (Program Physique et Chimie du Vivant), the Ministère de l‘Enseignement Supérieur, de la Recherche et de la Technologie (ACC-SDV5), and the Medical Research Council of Canada. K.P. is a Natural Sciences and Engineering Research Council of Canada University Research Fellow.

    *

     To whom correspondence should be addressed. E-mail:  schalk@ esbs.u-strasbg.fr. Phone:  (33) 03 88 65 52 73. Fax: (33) 03 88 65 52 98.

    ‡

     UPR 9050 CNRS.

    §

     Academy of Sciences of the Czech Republic.

    ‖

     Institut de Pharmacologie et de Biologie Structurale.

    ⊥

     Laboratoire de Spectrométrie de Mass Bio-organique.

    #

     Queen's University.

    Cited By

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    This article is cited by 69 publications.

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    Biochemistry

    Cite this: Biochemistry 1999, 38, 29, 9357–9365
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi990421x
    Published June 30, 1999
    Copyright © 1999 American Chemical Society
    Request reuse permissions

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