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Chapter 19 :

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Abstract:

spp., which are gram-negative bacilli that typically inhabit terrestrial and aquatic environs, have gained notoriety as important human, animal, and plant pathogens, as well as agents of biocontrol. Among the pseudomonads, is clearly the most significant as regards infectious disease in humans, generally causing opportunistic infections in individuals with compromised host defenses. The closely related phytopathogen, (formerly ) , is similarly resistant to many antimicrobials and also causes opportunistic and potentially debilitating infections in the lungs of cystic fibrosis (CF) patients as well as in individuals with chronic granulomatous disease. Pyoverdine (also called pseudobactin when found in rhizosphere pseudomonads such as and is responsible for the characteristic fluorescence of and, indeed, all fluorescent pseudomonads. Cell density has also been implicated in the control of pyoverdine production, with defects in quorum sensing correlating with a reduction in pyoverdine levels and pyoverdine biosynthetic gene expression, possibly because PvdS is itself positively regulated by quorum sensing. In any case, it is clear that siderophore-dependent expression of cognate transport genes is a common theme in , involving both endogenous and heterologous siderophores. While the study of iron acquisition in has, for the most part, focused on planktonic organisms, biofilms may well be the predominant mode of growth of the organism in nature.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19

Key Concept Ranking

Gene Expression and Regulation
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Outer Membrane Proteins
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Figures

Image of FIGURE 1
FIGURE 1

Pyoverdines of .

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 2
FIGURE 2

Endogenous siderophores of and spp.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 3
FIGURE 3

Heterologous bacterial siderophores used by .

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 4
FIGURE 4

Genetic organization of known pyoverdine biosynthetic genes (see Table 1 for their description) within the locus. Gene designations are given below the genes, and their corresponding PA designations ( Genome Project; http://www.pseudomonas.com) are shown above. Genes whose expression is positively impacted by PvdS are shown in white. Where present, iron starvation (IS, solid squares) and Fur (hatched squares) boxes are shown upstream of the biosynthetic genes. Intervening DNA is indicated by double vertical lines, while the open reading frames present within this intervening region are identified by their PA designations.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 5
FIGURE 5

Schematic showing pyoverdine-dependent expression of its cognate biosynthetic () and receptor () genes in . In the absence of pyoverdine (left), the ECF sigma factors necessary for (FpvI) and (PvdS) expression are sequestered by the anti-sigma factor FpvR and are unavailable to stimulate and gene expression. In the presence of pyoverdine (right), the iron complex of this siderophore interacts with its outer membrane receptor, FpvA, causing a conformational change that results in the release of the sigma factors by FpvR. These are then free to directRNApolymerase (RNAP) to the and genes and other pyoverdine-regulated genes. Note that the known PvdS/pyoverdine involvement in (exotoxin A) expression is apparently mediated by the RegA transcriptional activator. OM, outer membrane; PP, periplasm; CM, cytoplasmic membrane.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 6
FIGURE 6

Schematic showing pyochelin-dependent expression of its cognate biosynthetic () and receptor () genes in . In the absence of pyochelin (left), the regulatory protein, PchR, exists in a repressor form (R) and blocks the expression of and, possibly, the pyochelin biosynthetic genes. In the presence of pyochelin (right) or, more probably, ferric pyochelin, PchR is converted to a transcriptional activator (A) of the receptor and biosynthetic genes. It is unclear, however, whether ferric pyochelin is a direct effector of PchR activator activity, following its transport across the cytoplasmic membrane via a hitherto unknown carrier, or whether it simply interacts with its receptor, FptA, on the cell surface and this is signaled to PchR via an as yet undiscovered signal transduction pathway. OM, outer membrane; PP, periplasm; CM, cytoplasmic membrane.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 7
FIGURE 7

Schematic showing enterobactin-dependent expression of its cognate receptor gene in . Ferric enterobactin that is deposited in the periplasm by the PfeA receptor interacts with the PfeS sensor kinase, which ultimately phosphorylates the response regulator, PfeR, thereby activating it to drive the expression of the gene. This process is independent of any transport of the ferric siderophore complex across the cytoplasmic membrane by permease components (FepBCDG). A second receptor able to accommodate ferric enterobactin, PirA, has been proposed to explain ferric enterobactin uptake and stimulation of PfeSR in the absence of PfeA. Apparently associated with its own phosphorelay two-component regulatory system, PirSR, it is likely that PirA also transports another, as yet unknown, siderophore as its primary substrate and that this provides for up regulation, via PirSR, of the gene. OM, outer membrane; PP, periplasm; CM, cytoplasmic membrane.

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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Image of FIGURE 8
FIGURE 8

Schematic showing siderophore-mediated iron uptake in with a proposed common transporter for Fe operating at the cytoplasmic membrane. Siderophore-specific receptors are responsible for transport of the various iron-siderophore complexes across the outer membrane into the periplasm, where Fe is released as Fe (via a reductive mechanism) or Fe by an as yet unknown mechanism. Transporters specific for Fe (PA0369/PA0358) or Fe (PA5216/PA5217; PA4687/PA4688) are then responsible for transport across the inner membrane. CIT, citrate; PCH, pyochelin; PVD, pyoverdine; FOX, ferrioxamine B. The PA designations are those reported by the Genome Project (http://www.pseudomonas.com).

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
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References

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Tables

Generic image for table
TABLE 1

Genetics of pyoverdine biosynthesis

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
Generic image for table
TABLE 2

Known and putative iron receptors and their regulators in

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19
Generic image for table
TABLE 3

Genetics of pyochelin biosynthesis

Citation: Poole K. 2004. , p 293-310. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch19

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