Unexpected Interaction of a Siderophore with Aluminum and Its Receptor

Cornélis, Pierre

doi:10.1128/jb.00954-08

Cited by 16 publications

(12 citation statements)

References 22 publications

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“…Internalized PVD is recycled by the PvdRT-OpmQ system. It is hypothesized that Fe(II) enters the cytoplasm by a classic periplasmic binding protein (PBP)/IM ABC importer (15). Experimentally confirmed and hypothetical steps are in yellow and gray, respectively.…”

Section: Methodsmentioning

confidence: 99%

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Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa

Imperi

Tiburzi

Visca

2009

Proc. Natl. Acad. Sci. U.S.A.

200

219

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The siderophore pyoverdine (PVD) is a primary virulence factor of the human pathogenic bacterium Pseudomonas aeruginosa, acting as both an iron carrier and a virulence-related signal molecule. By exploring a number of P. aeruginosa candidate systems for PVD secretion, we identified a tripartite ATP-binding cassette efflux transporter, here named PvdRT-OpmQ, which translocates PVD from the periplasmic space to the extracellular milieu. We show this system to be responsible for recycling of PVD upon internalization by the cognate outer-membrane receptor FpvA, thus making PVD virtually available for new cycles of iron uptake. Our data exclude the involvement of PvdRT-OpmQ in secretion of de novo synthesized PVD, indicating alternative pathways for PVD export and recycling. The PvdRT-OpmQ transporter is one of the few secretion systems for which substrate recognition and extrusion occur in the periplasm. Homologs of the PvdRT-OpmQ system are present in genomes of all fluorescent pseudomonads sequenced so far, suggesting that PVD recycling represents a general energysaving strategy adopted by natural Pseudomonas populations.ATP-binding-cassette transporter ͉ periplasm ͉ iron ͉ fluorescent Pseudomonas ͉ secretion

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Section: Methodsmentioning

confidence: 99%

“…Iron release from PVD has been shown to occur in the periplasm, and that apo-PVD is then recycled to the extracellular milieu (13,14). However, no protein candidates have been proposed for these processes and further studies are required to elucidate the fate of iron and PVD following dissociation in the periplasm (15).…”

mentioning

confidence: 99%

Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa

Imperi

Tiburzi

Visca

2009

Proc. Natl. Acad. Sci. U.S.A.

200

219

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“…The ligand properties of enterobactin toward trivalent species (Al III , Ga III , Sc III , In III ),349 and the crystal structure of a enterobactin‐V IV complex have been reported 350. Other natural hydroxamate‐catechol siderophores such as pyoverdin and azoverdin have been shown to form stable coordination complexes with Ga III , Al III ,351, 352 and UO 2 2+ 353. These complexes are so stable that the presence of Al III and Ga III interfere with Fe III absorption in biological media 351.…”

Section: Siderophore‐like Materialsmentioning

confidence: 99%

Catechol‐Based Biomimetic Functional Materials

Saiz‐Poseu²,

et al. 2012

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Abstract.Catechols are found in nature taking part in a remarkably broad scope of biochemical processes and functions. Though not exclusively, such versatility may be traced back to several properties uniquely found together in the o -dihydroxyaryl chemical function; namely, its ability to establish reversible equilibria at moderate redox potentials and pHs and to irreversibly cross-link through complex oxidation mechanisms; its excellent chelating properties, greatly exemplifi ed by, but by no means exclusive, to the binding of Fe 3 + ; and the diverse modes of interaction of the vicinal hydroxyl groups with all kinds of surfaces of remarkably different chemical and physical nature. Thanks to this diversity, catechols can be found either as simple molecular systems, forming part of supramolacular structures, coordinated to different metal ions or as macromolecules mostly arising from polymerization mechanisms through covalent bonds. Such versatility has allowed catechols to participate in several natural processes and functions that range from the adhesive properties of marine organisms to the storage of some transition metal ions. As a result of such an astonishing range of functionalities, catechol-based systems have in recent years been subject to intense research, aimed at mimicking these natural systems in order to develop new functional materials and coatings. A comprehensive review of these studies is discussed in this paper.

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“…Microbial systems are also known to devise various stratagems to nullify the toxicity of Al. The immobilization of the metal in the cell wall, its sequestration into exopolysaccharides, its entrapment intracellularly and its complexation with siderophores enable microbes to survive Al stress (Cervantes and Silver, 1996; Cornelis, 2008). The latter strategy may indeed further interfere with Fe metabolism.…”

Section: Al Interferes With Fe Homeostasismentioning

confidence: 99%