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GUEST COMMENTARIES

Unexpected Interaction of a Siderophore with Aluminum and Its Receptor

Pierre Cornelis
Pierre Cornelis
Microbial Interactions, Department of Molecular and Cellular Interactions, Flanders Institute for Biotechnology (VIB) and Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium
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  • For correspondence: pcornel@vub.ac.be
DOI: 10.1128/JB.00954-08
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    FIG. 1.

    Hypothetical model of ferripyoverdine uptake by FpvA (TonB and ExbBD are not shown for clarity) based on the discovery of rapid recycling of pyoverdine (PVD), suggesting that it is not transported to the cytoplasm (5, 14, 15). Ferripyoverdine is bound to FpvA and is transported via the proton motive force relayed by TonB; once it is in the periplasm, a still-undescribed reduction process takes place and Fe2+ is bound to a periplasmic binding protein which delivers it to an ABC transporter. Ga-pyoverdine and Al-pyoverdine also can be transported but are not further processed in the periplasm.

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Unexpected Interaction of a Siderophore with Aluminum and Its Receptor
Pierre Cornelis
Journal of Bacteriology Sep 2008, 190 (20) 6541-6543; DOI: 10.1128/JB.00954-08

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Unexpected Interaction of a Siderophore with Aluminum and Its Receptor
Pierre Cornelis
Journal of Bacteriology Sep 2008, 190 (20) 6541-6543; DOI: 10.1128/JB.00954-08
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  • Top
  • Article
    • SIDEROPHORES DO NOT BIND ONLY IRON
    • MECHANISM OF FERRIPYOVERDINE UPTAKE
    • FATE OF FERRIPYOVERDINE AND RECYCLING OF APO-PYOVERDINE
    • REFERENCES
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KEYWORDS

Aluminum
Bacterial Outer Membrane Proteins
Oligopeptides
Pseudomonas aeruginosa

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