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.

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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