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Chapter 20 :

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Abstract:

, , and are mammalian respiratory pathogens that are highly genetically related gram-negative β-proteobacteria of the family . This chapter summarizes the current knowledge of iron acquisition in , and although it is not possible to cite all of the works by investigators in the field, their research contributions have been critical to the development of this knowledge base. toxins may alter the integrity of the epithelium, allowing serum components such as complement, and possibly lymphocytes and erythrocytes, to breach the mucosa. The alcaligin system gene cluster spans an approximately 11-kb genomic region and includes the ABCDER operon and the and genes. Transcriptional activation of genes by is remarkably sensitive to the presence of purified deferri-alcaligin inducer. The current understanding of these systems suggests the following model for gene regulation. One study using regulator mutants failed to demonstrate an effect of mutation on mouse virulence, but since mutants retain some low-level capacity to produce and transport alcaligin, this result did not eliminate the possibility that alcaligin utilization contributes to virulence. The authors postulate that the ability of species to selectively activate the expression of the different iron systems contributes to its capacity to effectively adapt and multiply in the host environment during the course of an infection.

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20

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Two-Component Signal Transduction Systems
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Nuclear Magnetic Resonance Spectroscopy
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Figures

Image of FIGURE 1
FIGURE 1

Molecular structure of alcaligin.

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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Image of FIGURE 2
FIGURE 2

Genetic organization of the alcaligin siderophore system. Arrows indicate the transcriptional orientations and spatial limits of genes, and open circles represent known Fur-regulated promoter-operator regions. Known AlcR-responsive control regions reside upstream of and . has been renamed .

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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Image of FIGURE 3
FIGURE 3

Enterobactin-inducible BfeA receptor protein production. Production of the ~80-kDa BfeA ferric enterobactin receptor protein was monitored by immunoblot analysis of and total proteins by using a cross-reactive FepA-specific antiserum. Lanes: +Iron, iron-replete culture; −Iron, iron-depleted culture; −Iron +Ent, iron-depleted culture supplemented with enterobactin; −Iron +Alc, iron-depleted culture supplemented with alcaligin.

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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Image of FIGURE 4
FIGURE 4

Genetic organization of the enterobactin utilization system. Arrows indicate the spatial limits and transcriptional orientations of the genes, and open circles designate the positions of predicted Fur-binding sites upstream from and .

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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Image of FIGURE 5
FIGURE 5

Genetic organization of the heme iron utilization system. Arrows indicate the transcriptional orientations and spatial limits of genes, and open circles designate the positions of predicted promoter regions. A Fur-binding site resides upstream of , and a predicted ECF σ factor-dependent promoter is upstream of .

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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Image of FIGURE 6
FIGURE 6

Heme-inducible BhuR receptor protein production. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of membrane fractions of a wildtype (wt) strain and an isogenic null mutant cultured under iron-depleted conditions (−Fe) and iron-depleted conditions with hemin supplementation (5 µM) (−Fe +Hm) is shown. Positions of molecular mass markers (in kilodaltons) and BhuR (arrowheads) are indicated. Adapted from Vanderpool and Armstrong (2001) with permission.

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
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References

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1. Beall, B.,, and G. N. Sanden. 1995. A Bordetella pertussis fepA homologue required for utilization of exogenous ferric enterobactin. Microbiology 141: 3193 3205.
2. Beaumont, F. C.,, H. Y. Kang,, T. J. Brickman,, and S. K. Armstrong. 1998. Identification and characterization of alcR, a gene encoding an AraClike regulator of alcaligin siderophore biosynthesis and transport in Bordetella pertussis and Bordetella bronchiseptica. J. Bacteriol. 180: 862 870.
3. Braun, V. 1997. Surface signaling: novel transcription initiation mechanism starting from the cell surface. Arch. Microbiol. 167: 325 331.
4. Brickman, T. J.,, and S. K. Armstrong. 2002. Bordetella interspecies allelic variation in AlcR inducer requirements: identification of a critical determinant of AlcR inducer responsiveness and construction of an alcR(Con) mutant allele. J. Bacteriol. 184: 1530 1539.
5. Brickman, T. J.,, H. Y. Kang,, and S. K. Armstrong. 2001. Transcriptional activation of Bordetella alcaligin siderophore genes requires the AlcR regulator with alcaligin as inducer. J. Bacteriol. 183: 483 489.
6. Brickman, T. J.,, J.-G. Hansel,, M. J. Miller,, and S. K. Armstrong. 1996. Purification, spectroscopic analysis, and biological activity of the macrocyclic dihydroxamate siderophore alcaligin produced by Bordetella pertussis and Bordetella bronchiseptica. Bio- Metals 9: 191 203.
7. Giardina, P. C.,, L. A. Foster,, S. I. Toth,, B. A. Roe,, and D. W. Dyer. 1997. Analysis of the alcABC operon encoding alcaligin biosynthesis enzymes in Bordetella bronchiseptica. Gene 194: 19 24.
8. Gorringe, A. R.,, G. Woods,, and A. Robinson. 1990. Growth and siderophore production by Bordetella pertussis under iron-restricted conditions. FEMS Microbiol. Lett. 66: 101 106.
9. Hou, Z.,, C. J. Sunderland,, T. Nishio,, and K. N. Raymond. 1996. Preorganization of ferric alcaligin, Fe2L3. The first structure of a ferric dihydroxamate siderophore. J. Am. Chem. Soc. 118: 5148 5149.
10. Kang, H. Y.,, and S. K. Armstrong. 1998. Transcriptional analysis of the Bordetella alcaligin siderophore biosynthesis operon. J. Bacteriol. 180: 855 861.
11. Kirby A. E,, N. D. King,, and T. D. Connell. 2004. RhuR, an extracytoplasmic function sigma factor activator, is essential for heme-dependent expression of the outer membrane heme and hemoprotein receptor of Bordetella avium. Infect. Immun. 72: 896 907.
12. Locht, C.,, R. Antoine,, and F. Jacob-Dubuisson. 2001. Bordetella pertussis, molecular pathogenesis under multiple aspects. Curr. Opin. Microbiol. 4: 82 89.
13. Moore, C. H.,, L. A. Foster,, J. G. Gerbig,, D. W. Dyer,, and B. W. Gibson. 1995. Identification of alcaligin as the siderophore produced by Bordetella pertussis and Bordetella bronchiseptica. J. Bacteriol. 177: 1116 1118.
14. Murphy, E. R.,, R. E. Sacco,, A. Dickenson,, D. J., Metzger,, Y. Hu,, P. E. Orndorff,, and T. D. Connell. 2002. BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins. Infect. Immun. 70: 5390 5403.
15. Nicholson, M. L.,, and B. Beall. 1999. Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin as iron sources. Microbiology 145: 2453 2461.
16. Nishio, T.,, N. Tanaka,, J. Hiratake,, Y. Katsube,, Y. Ishida,, and J. Oda. 1988. Isolation and struc ture of the novel dihydroxamate siderophore alcaligin. J. Am. Chem. Soc. 110: 8833 8734.
17. Pradel, E.,, and C. Locht. 2001. Expression of the putative siderophore receptor gene bfrZ is controlled by the extracytoplasmic-function sigma factor BupI in Bordetella bronchiseptica. J. Bacteriol. 183: 2910 2917.
18. Pradel, E.,, N. Guiso,, and C. Locht. 1998. Identification of AlcR, an AraC-type regulator of alcaligin siderophore synthesis in Bordetella bronchiseptica and Bordetella pertussis. J. Bacteriol. 180: 871 880.
19. Redhead, K.,, T. Hill,, and H. Chart. 1987. Interaction of lactoferrin and transferrins with the outer membrane of Bordetella pertussis. J. Gen. Microbiol. 133: 891 898.
20. Register K. B.,, T. F. Ducey,, S. L. Brockmeier,, and D. W. Dyer. 2001. Reduced virulence of a Bordetella bronchiseptica siderophore mutant in neonatal swine. Infect. Immun. 69: 2137 2143.
21. Vanderpool, C. K.,, and S. K. Armstrong 2001. The Bordetella bhu locus is required for heme iron utilization. J. Bacteriol. 183: 4278 4287.

Tables

Generic image for table
TABLE 1

alcaligin system proteins and homologs

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
Generic image for table
TABLE 2

enterobactin utilization system proteins and homologs

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20
Generic image for table
TABLE 3

heme iron utilization system proteins and homologs

Citation: Brickman T, Vanderpool C, Armstrong S. 2004. , p 311-328. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch20

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