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Pyoverdine (PVDI) has been reported to act both as a siderophore for scavenging iron (a key nutrient) and a signaling molecule for the expression of virulence factors. This compound is itself part of a core set of virulence factors produced by  Pseudomonas aeruginosa  during infections. Once secreted into the bacterial environment and having scavenged ferric iron, PVDI-Fe 3+  is taken back into the  P. aeruginosa  periplasm via the outer membrane transporters FpvAI and FpvB. Iron release from PVDI in the bacterial periplasm involves numerous proteins encoded by the  fpvGHJKCDEF  genes and a mechanism of iron reduction. Here, we investigated the global interacting network between these various proteins using systematic bacterial two-hybrid screening. We deciphered a network of five interacting proteins composed of two inner-membrane proteins, FpvG (iron reductase) and FpvH (unknown function), and three periplasmic proteins, FpvJ (unknown function), FpvF (periplasmic PVDI-binding protein), and FpvC (iron periplasmic-binding protein). This interacting network strongly suggests the existence of a large protein machinery composed of these five proteins, all playing a role in iron acquisition by PVDI. Furthermore, we discovered an interaction between the periplasmic siderophore binding protein FpvF and the PvdRT-OpmQ efflux pump, also suggesting a role for FpvF in apo-PVDI recycling and secretion after iron delivery. These results highlight a multi-protein complex that drives iron release from PVDI in the periplasm of  P. aeruginosa .

Iron acquisition in Pseudomonas aeruginosa by the siderophore pyoverdine: an intricate interacting network including periplasmic and membrane proteins