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1 University of Groningen;
2 University of Groningen and University of Surabaya;
3 Ghent University
PvdQ, an acylase from Pseudomonas aeruginosa PAO1, has been shown to have at least two functions. It can act as a quorum quencher in the light of its capability to degrade long-chain acyl homoserine lactones (AHLs) e.g. 3-oxo-C12-HSL, leading to a decrease in virulence factors. In addition, PvdQ is involved in iron homeostasis by playing a role in the biosynthesis of pyoverdine, the major siderophore of P. aeruginosa. In accordance with earlier studies on RNA level, we could show at protein level that PvdQ is only expressed when iron is present at very low concentrations. Consequently, we have set out to investigate the two functions of PvdQ under iron limiting conditions. Gene deletion of pvdQ does not affect growth of P. aeruginosa but abrogates pyoverdine production, and results in an accumulation of 3-oxo-C12-HSL. Phenotypical analyses of our deletion mutant at low iron concentrations revealed that _pvdQ is impaired in swarming motility and biofilm formation. Additionally, a plant and a C. elegans infection model demonstrated that the deletion of pvdQ resulted in reduced virulence. None of the phenotypes in the present study could be linked to the presence or absence of AHLs. These results clearly indicate that under iron limiting conditions PvdQ plays a major role in swarming motility, in biofilm development and in infection that is more likely to be linked to the pyoverdine pathway rather than the LasI/LasR/3-oxo-C12-HSL quorum sensing circuit.
4 E-mail: w.j.quax{at}rug.nl
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