1887

Chapter 20 :

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap20-1.gif /docserver/preview/fulltext/10.1128/9781555816544/9781555812928_Chap20-2.gif

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

Key Concept Ranking

Two-Component Signal Transduction Systems
0.43359274
Nuclear Magnetic Resonance Spectroscopy
0.4089765
0.43359274
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint
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
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555816544.chap20
1. Beall, B.,, and G. N. Sanden. 1995. A Bordetella pertussis fepA homologue required for utilization of exogenous ferric enterobactin. Microbiology 141: 31933205.
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. 180:862870.
3. Braun, V. 1997. Surface signaling: novel transcription initiation mechanism starting from the cell surface. Arch. Microbiol. 167:325331.
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: 15301539.
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: 483489.
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 9:191203.
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: 1924.
8. Gorringe, A. R.,, G. Woods,, and A. Robinson. 1990. Growth and siderophore production by Bordetella pertussis under iron-restricted conditions. FEMS Microbiol. Lett. 66:101106.
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: 51485149.
10. Kang, H. Y.,, and S. K. Armstrong. 1998. Transcriptional analysis of the Bordetella alcaligin siderophore biosynthesis operon. J. Bacteriol. 180: 855861.
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: 896907.
12. Locht, C.,, R. Antoine,, and F. Jacob-Dubuisson. 2001. Bordetella pertussis, molecular pathogenesis under multiple aspects. Curr. Opin. Microbiol. 4: 8289.
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: 11161118.
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. 70:53905403.
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: 24532461.
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. 110:88338734.
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: 29102917.
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. 180:871880.
19. Redhead, K.,, T. Hill,, and H. Chart. 1987. Interaction of lactoferrin and transferrins with the outer membrane of Bordetella pertussis. J. Gen. Microbiol. 133:891898.
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. 69:21372143.
21. Vanderpool, C. K.,, and S. K. Armstrong 2001. The Bordetella bhu locus is required for heme iron utilization. J. Bacteriol. 183:42784287.

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

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error