Genomics of the 35-kb pvd locus and analysis of novel pvdIJK genes implicated in pyoverdine biosynthesis in Pseudomonas aeruginosa

Lehoux, D

doi:10.1016/s0378-1097(00)00314-1

Cited by 34 publications

(44 citation statements)

References 15 publications

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“…output ratio of mutant when compared to wild-type strain, divided by the c.f.u. input ratio of mutant to wild-type strain (Lehoux et al, 2000). The final CI was calculated as the geometric mean for animals in the same group, and experiments were done at least in triplicate (Hava & Camilli, 2002).…”

Section: Methodsmentioning

confidence: 99%

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

et al. 2009

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Pseudomonas aeruginosa is a ubiquitous environmental Gram-negative bacterium that is also a major opportunistic human pathogen in nosocomial infections and cystic fibrosis chronic lung infections. PhoP-PhoQ is a two-component regulatory system that has been identified as essential for virulence and cationic antimicrobial peptide resistance in several other Gram-negative bacteria. This study demonstrated that mutation of phoQ caused reduced twitching motility, biofilm formation and rapid attachment to surfaces, 2.2-fold reduced cytotoxicity to human lung epithelial cells, substantially reduced lettuce leaf virulence, and a major, 10 000-fold reduction in competitiveness in chronic rat lung infections. Microarray analysis revealed that PhoQ controlled the expression of many genes consistent with these phenotypes and with its known role in polymyxin B resistance. It was also demonstrated that PhoQ controls the expression of many genes outside the known PhoP regulon.

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Section: Methodsmentioning

confidence: 99%

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

et al. 2009

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“…These genes are thought to encode peptide synthetases (Lehoux et al, 2000;Merriman et al, 1995), a family of proteins with many conserved sequence features . PvdD directs incorporation of two L-threonine residues into pyoverdine PAO (Ackerley et al, 2003) and pvdI and pvdJ are very likely to encode peptide synthetases that direct incorporation of the remaining six amino acids into the peptide of type I pyoverdines.…”

Section: Detection Of Pvd Gene Homologues In Other Pseudomonas Strainsmentioning

confidence: 99%

“…The product of the pvdD gene is a peptide synthetase that directs incorporation of two L-threonine residues into the peptide of pyoverdine PAO Ackerley et al, 2003). The pvdIJK gene products also have the characteristics of peptide synthetases (Lehoux et al, 2000); resequencing of P. aeruginosa PAO1 DNA shows that pvdJ and pvdK are part of a single gene (see below), which will be referred to here as pvdJ. The product of the pvdE gene is likely to be an ABC transporter protein and it is essential for pyoverdine synthesis (McMorran et al, 1996) although the transported substrate has not been identified.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of novel pyoverdine synthesis genes in Pseudomonas aeruginosa

2003

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Fluorescent pseudomonads secrete yellow-green siderophores named pyoverdines or pseudobactins. These comprise a dihydroxyquinoline derivative joined to a type-specific peptide and, usually, a carboxylic acid or amide. In Pseudomonas aeruginosa strain PAO1, six genes that encode proteins required for pyoverdine synthesis (pvd genes) have been identified previously. Expression of all of these genes requires an alternative sigma factor PvdS. The purpose of this research was to identify other genes that are required for pyoverdine synthesis in P. aeruginosa PAO1. Fourteen candidate genes were identified from the PAO1 genome sequence on the basis of their location in the genome, the functions of homologues in other bacteria, and whether their expression was likely to be PvdS-dependent. The candidate genes were mutated and the effects of the mutations on pyoverdine production were determined. Eight new pvd genes were identified. The presence of homologues of pvd genes in other strains of P. aeruginosa was determined by Southern blotting and in other fluorescent pseudomonads by interrogation of genome sequences. Five pvd genes were restricted to strains of P. aeruginosa that make the same pyoverdine as strain PAO1, suggesting that they direct synthesis of the type-specific peptide. The remaining genes were present in all strains of P. aeruginosa that were examined and homologues were present in other Pseudomonas species. These genes are likely to direct synthesis of the dihydroxyquinoline moiety and the attached carboxylic acid/amide group. It is likely that most if not all of the genes required for pyoverdine synthesis in P. aeruginosa PAO1 have now been identified and this will form the basis for a biochemical description of the pathway of pyoverdine synthesis.

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“…PVDs are composed of a conserved dihydroxyquinoline chromophore, a variable peptide chain, comprising 6-12 amino acids, specific to a producing strain, and a side-chain, generally a dicarboxylic acid or an amide (Ravel & Cornelis, 2003). Both the chromophore and the peptide chain of PVDs are synthesized by non-ribosomal peptide synthetases (Merriman et al, 1995;Lehoux et al, 2000;Mossialos et al, 2002). Ferribactin, the precursor of PVD, is probably exported to the periplasm where it is matured into PVD with a chromophore .…”

Section: Introductionmentioning

confidence: 99%

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

et al. 2003

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The cytoplasmic membrane protein CcmC is, together with other Ccm proteins, a component for the maturation of c-type cytochromes in Gram-negative bacteria. A Pseudomonas fluorescens ATCC 17400 ccmC mutant is cytochrome c-deficient and shows considerably reduced production of the two siderophores pyoverdine and quinolobactin, paralleled by a general inability to utilize various iron sources, with the exception of haem. The ccmC mutant accumulates in a 5-aminolevulinic acid-dependent synthesis a reddish, fluorescent pigment identified as protoporphyrin IX. As a consequence a visA phenotype similar to that of a ferrochelatase-deficient hemH mutant characterized by drastically reduced growth upon light exposure was observed for the ccmC mutant. The defect of iron–protoporphyrin formation was further demonstrated by the failure of ccmC cell-free proteinase K-treated extracts to stimulate the growth of a haem auxotrophic hemH indicator strain, compared to similarly prepared wild-type extracts. In addition, the ccmC mutant did not sustain hemH growth in cross-feeding experiments while the wild-type did. Significantly reduced resistance to oxidative stress mediated by haem-containing catalases was observed for the ccmC mutant. A double hemH ccmC mutant could not be obtained in the presence of external haem without the hemH gene in trans, indicating that the combination of the two mutations is lethal. It was concluded that CcmC, apart from its known function in cytochrome c biogenesis, plays a role in haem biosynthesis. A function in the regulatory co-ordination of iron acquisition via siderophores, iron insertion into porphyrin via ferrochelatase and iron–protoporphyrin export for cytochrome c formation is predicted.

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Genomics of the 35-kb pvd locus and analysis of novel pvdIJK genes implicated in pyoverdine biosynthesis in Pseudomonas aeruginosa

Cited by 34 publications

References 15 publications

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

Identification and characterization of novel pyoverdine synthesis genes in Pseudomonas aeruginosa

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

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