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Chapter 6 : Iron Requirements of and Acquisition of Iron by

Authors: Nicholas P. Cianciotto1, Sherry Kurtz1, Kevin Krcmarik1, Sejal Mody1, Uttara Prasad1, Marianne Robey1, Joseph Salerno1, V. K. Viswanathan1
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Affiliations: 1: Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, IL 60611
Content Type: Monograph
Publication Year: 2002

Category: Bacterial Pathogenesis

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Abstract:

This chapter discusses the current understanding of the relationship between and the metal iron. It summarizes the work of a number of laboratories that demonstrated the importance of iron for , and highlights recent advances toward uncovering mechanisms of iron acquisition. The mutant displayed a 42% reduction in hemin binding, confirming that potentiates hemin acquisition by . Within U937 cells, NU216 and its allelic equivalent NU216R were approximately 100-fold more sensitive than the wild type to treatment with desferoxamine, confirming that they are defective for intracellular iron acquisition. The EDDA-hypersensitive mutant NU208 was also dramatically impaired for replication in U937 cells, and its infectivity defect was exacerbated by treatment of the macrophages with desferoxamine. A reconstruction of the NU208 mutation confirmed that the iron acquisition and infectivity defects were due to the transposon insertion and not a spontaneous second-site mutation. Sequence analysis demonstrated that the transposon disruption lies within a gene that is highly similar to the cytochrome c maturation gene, . is generally recognized for its role in the heme export step of cytochrome biogenesis. Quantitative infection assays demonstrated that NU229 was impaired ca. 80-fold in intracellular growth. Reconstruction of the mutant by allelic exchange proved that the defect was due to the inactivation of frgA and not a spontaneous second-site mutation. Subsequently, trans-complementation of the mutation demonstrated that the infectivity defect was directly due to the loss of FrgA.

Citation: Cianciotto N, Kurtz S, Krcmarik K, Mody S, Prasad U, Robey M, Salerno J, Viswanathan V. 2002. Iron Requirements of and Acquisition of Iron by , p 31-37. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch6
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Iron Requirements of and Acquisition of Iron by Legionella pneumophila
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Citation: Cianciotto N, Kurtz S, Krcmarik K, Mody S, Prasad U, Robey M, Salerno J, Viswanathan V. 2002. Iron Requirements of and Acquisition of Iron by , p 31-37. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch6
/content/10.1128/9781555817985.chap6.fig6-1
FIGURE 1

Potential iron acquisition pathways of . See text for details.

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10.1128/9781555817985/fig6-1.gif
Image of FIGURE 1
FIGURE 1

Potential iron acquisition pathways of . See text for details.

Citation: Cianciotto N, Kurtz S, Krcmarik K, Mody S, Prasad U, Robey M, Salerno J, Viswanathan V. 2002. Iron Requirements of and Acquisition of Iron by , p 31-37. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch6
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References

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1. Bortner, C. A.,, R. R. Arnold,, and R. D. Miller. 1989. Bactericidal effect of lactoferrin on Legionella pneumophila: effect of the physiological state of the organism. Can. J. Microbiol. 35: 1048– 1051.
2. Byrd, T. F.,, and M. A. Horwitz. 1989. Interferon gamma-activated human monocytes downregulate transferrin receptors and inhibit the intracellular multiplication of Legionella pneumophila by limiting the availability of iron. J. Clin. Invest. 83: 1457– 1465.
3. Byrd, T. F.,, and M. A. Horwitz. 1991. Lactoferrin inhibits or promotes Legionella pneumophila intracellular multiplication in nonactivated and interferon gamma-activated human monocytes depending upon its degree of iron saturation. Iron-lactoferrin and nonphysiologic iron chelates reverse monocyte activation against Legionella pneumophila. J. Clin. Invest. 88: 1103– 1112.
4. Clemens, D. L.,, and M. A. Horwitz. 1995. Characterization of the Mycobacterium tuberculosis phagosome and evidence that phagosomal maturation is inhibited. J. Exp. Med. 181: 257– 270.
5. Gebran, S. J.,, C. Newton,, Y. Yamamoto,, R. Widen,, T. W. Klein,, and H. Friedman. 1994. Macrophage permissiveness for Legionella pneumophila growth modulated by iron. Infect. Immun. 62: 564– 568.
6. Goldoni, P.,, P. Visca,, M. C. Pastoris,, P. Valenti,, and N. Orsi. 1991. Growth of Legionella spp. under conditions of iron restriction. J. Med. Microbiol. 34: 113– 118.
7. Hickey, E. K.,, and N. P. Cianciotto. 1994. Cloning and sequencing of the Legionella pneumophila fur gene. Gene 143: 117– 121.
8. Hickey, E. K.,, and N. P. Cianciotto. 1997. An iron- and fur-repressed Legionella pneumophila gene that promotes intracellular infection and encodes a protein with similarity to the Escherichia coli aerobactin synthetases. Infect. Immun. 65: 133– 143.
9. James, B. W.,, W. S. Mauchline,, P. J. Dennis,, and C. W. Keevil. 1997. A study of iron acquisition mechanisms of Legionella pneumophila grown in chemostat culture. Curt. Microbiol. 34: 238– 243.
10. James, B. W.,, W. S. Mauchline,, R. B. Fitzgeorge,, P. J. Dennis,, and C. W. Keevil. 1995. Influence of iron-limited continuous culture on physiology and virulence of Legionella pneumophila. Infect. Immun. 63: 4224– 4230.
11. Johnson, W.,, L. Varaer,, and M. Poch. 1991. Acquisition of iron by Legionella pneumophila: role of iron reductase. Infect. Immun. 59: 2376– 2381.
12. Liles, M. R.,, T. Aber Scheel,, and N. P. Cianciotto. 2000. Discovery of a nonclassical siderophore, legiobactin, produced by strains of Legionella pneumophila. J. Bacteriol. 182: 749– 757.
13. Liles, M. R.,, and N. P. Cianciotto. 1996. Absence of siderophore-like activity in Legionella pneumophila supematants. Infect. Immun. 64: 1873– 1875.
14. Mengaud, J. M.,, and M. A. Horwitz. 1993. The major iron-containing protein of Legionella pneumophila is an aconitase homologous with the human iron-responsive element-binding protein. J. Bacteriol. 175: 5666– 5676.
15. O'Connell, W. A.,, E. E. Hickey,, and N. P. Cianciotto. 1996. A Legionella pneumophila gene that promotes hemin binding. Infect. Immun. 64: 842– 848.
16. Poch, M. T.,, and W. Johnson. 1993. Ferric reductases of Legionella pneumophila. Biometals 6: 107– 114.
17. Pope, C. D.,, W. O'Connell,, and N. P. Cianciotto. 1996. Legionella pneumophila mutants that are defective for iron acquisition and assimilation and intracellular infection. Infect. Immun. 64: 629– 636.
18. Quinn, F. D.,, and E. D. Weisberg. 1988. Killing of Legionella pneumophila by human serum and iron-binding agents. Curr. Microbiol. 17: 111– 116.
19. Reeves, M. W.,, L. Pine,, J. B. Neilands,, and A. Balows. 1983. Absence of siderophore activity in Legionella species grown in iron-deficient media. J. Bacteriol. 154: 324– 329.
20. Viswanathan, V. K.,, P. H. Edelstein,, C. D. Pope,, and N. P. Cianciotto. 2000. The Legionella pneumophila iraAB locus is required for iron assimilation, intracellular infection, and virulence. Infect. Immun. 68: 1069– 1079.

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