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Updated: Jun 18, 2026

Qualitative and Quantitative Analysis of Siderophore Production from Pseudomonas aeruginosa
Published on: March 15, 2024
Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa
Francesco Imperi1, Federica Tiburzi, Paolo Visca
1Department of Biology, University Roma Tre, Viale G. Marconi 446, 00146 Roma, Italy.
Abstract:
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 energy-saving strategy adopted by natural Pseudomonas populations.
Insights
Pseudomonas aeruginosa uses pyoverdine (PVD) for iron uptake and virulence. A newly identified PvdRT-OpmQ transporter recycles internalized PVD, conserving this crucial molecule for bacteria.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Molecular Biology
Background:
- Pyoverdine (PVD) is a key virulence factor and iron siderophore for Pseudomonas aeruginosa.
- PVD functions as an iron carrier and a signaling molecule influencing bacterial virulence.
Purpose of the Study:
- To identify and characterize the P. aeruginosa system responsible for pyoverdine (PVD) secretion and recycling.
- To elucidate the mechanism of PVD translocation and its role in iron acquisition.
Main Methods:
- Exploration of candidate secretion systems in P. aeruginosa.
- Identification and characterization of the tripartite ATP-binding cassette (ABC) efflux transporter PvdRT-OpmQ.
- Analysis of PVD translocation from the periplasm to the extracellular environment.
Main Results:
- A tripartite ABC efflux transporter, PvdRT-OpmQ, was identified for PVD translocation.
- PvdRT-OpmQ mediates the recycling of internalized PVD via the FpvA receptor.
- This system is crucial for maintaining PVD availability for iron uptake but not for de novo secretion.
Conclusions:
- PvdRT-OpmQ facilitates PVD recycling, an energy-saving strategy for Pseudomonas aeruginosa.
- This transporter represents a periplasmic secretion system where substrate recognition and extrusion occur within the periplasm.
- Homologs of PvdRT-OpmQ suggest PVD recycling is a widespread mechanism in fluorescent pseudomonads.
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