Iron acquisition and metabolism by mycobacteria

Journal of Bacteriology

Volumn 181, Issue 15, 1999, Pages 4443-4451

  De Voss, James J ^a   Rutter, Kerry ^a   Schroeder, Benjamin G ^b   Barry III, Clifton E ^b  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IRON; PEPTIDE SYNTHASE; SIDEROPHORE;

BACTERIAL GROWTH; BIOSYNTHESIS; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; IRON METABOLISM; IRON STORAGE; MYCOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SHORT SURVEY;

BACTERIA (MICROORGANISMS); CORYNEBACTERINEAE; MYCOBACTERIUM;

EID: 0032765906     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.15.4443-4451.1999     Document Type: Short Survey

References (86)

1. Allen, M., A. J. Birch, and A. R. Jones. 1970. Studies in relation to biosynthesis. XLIII. Incorporation of L-lysine into mycobactin-P. Aust. J. Chem. 23:427-429.
2. Andrews, S. C. 1998. Iron storage in bacteria. Adv. Microb. Physiol. 40:281-351.
3. Barclay, R., D. F. Ewing, and C. Ratledge. 1985. Isolation, identification, and structural analysis of the mycobactins of Mycobacterium avium, Mycobacterium intracellulare, Mycobacterium scrofulaceum, and Mycobacterium paratuberculosis. J. Bacteriol. 164:896-903.
4. Barclay, R., and C. Ratledge. 1983. Iron-binding compounds of Mycobacterium avium, M. intracellulare, M. scrofulaceum, and mycobactin-dependent M. paratuberculosis and M. avium. J. Bacteriol. 153:1138-1146.
5. Baynes, R. D., H. Flax, T. H. Bothwell, W. R. Bezwoda, A. P. MacPhail, P. Atkinson, and D. Lewis. 1986. Haematological and iron-related measurements in active pulmonary tuberculosis. Scand. J. Haematol. 36:280-287.
6. Calder, K. M., and M. A. Horwitz. 1998. Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microb. Pathog. 24:133-143.
7. 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.
8. Cole, S. T., R. Brosch, J. Parkhill, T. Garnier, C. Churcher, D. Harris, S. V. Gordon, K. Eiglmeier, S. Gas, C. E. Barry III, F. Tekaia, K. Badcock, D. Basham, D. Brown, T. Chillingworth, R. Connor, R. Davies, K. Devlin, T. Feltwell, S. Gentles, N. Hamlin, S. Holroyd, T. Hornsby, K. Jagels, and B. G. Barrell. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544. (Erratum, 396:190, 1998.)
9. Crosa, J. H. 1997. Signal transduction and transcriptional and posttranscriptional control of iron-regulated genes in bacteria. Microbiol. Mol. Biol. Rev. 61:319-336.
10. De Voss, J. J., K. Rutter, Y. Zhu, B. G. Schroeder, and C. E. Barry III. The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Submitted for publication.
11. Dhople, A. M., M. A. Ibanez, and T. C. Poirier. 1996. Role of iron in the pathogenesis of Mycobacterium avium infection in mice. Microbios 87:77-87.
12. Douvas, G. S., M. H. May, and A. J. Crowle. 1993. Transferrin, iron, and serum lipids enhance or inhibit Mycobacterium avium replication in human macrophages. J. Infect. Dis. 167:857-864.
13. Dussurget, O., M. Rodriguez, and I. Smith. 1996. An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response. Mol. Microbiol. 22:535-544.
14. Fiss, E. H., S. Yu, and W. R. Jacobs, Jr. 1994. Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways. Mol. Miciobiol. 14:557-569.
15. Francis, J., H. M. Macturk, J. Madinaveitia, and G. A. Snow. 1953. Mycobactin, a growth factor for Mycobacterium johnei. I. Isolation from M. phlei. Biochem. J. 55:596-607.
16. Gehring, A. M., I. Mori, R. D. Perry, and C. T. Walsh. 1998. The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 37:11637-11650.
17. Gobin, J., and M. A. Horwitz. 1996. Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J. Exp. Med. 183:1527-1532.
18. Gobin, J., C. H. Moore, J. R. Reeve, Jr., D. K. Wong, B. W. Gibson, and M. A. Horwitz. 1995. Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc. Natl. Acad. Sci. USA 92:5189-5193.
19. Golden, C. A., I. Kochan, and D. R. Spriggs. 1974. Role of mycobactin in the growth and virulence of tubercle bacilli. Infect. Immun. 9:34-40.
20. Gordeuk, V. R., C. E. McLaren, A. P. MacPhail, G. Deichsel, and T. H. Bothwell. 1996. Associations of iron overload in Africa with hepatocellular carcinoma and tuberculosis: Strachan's 1929 thesis revisited. Blood 87:3470-3476.
21. Hardham, J. M., L. V. Stamm, S. F. Porcella, J. G. Frye, N. Y. Barnes, J. K. Howell, S. L. Mueller, J. D. Radolf, G. M. Weinstock, and S. J. Norris. 1997. Identification and transcriptional analysis of a Treponema pallidum operon encoding a putative ABC transport system, an iron-activated repressor protein homolog, and a glycolytic pathway enzyme homolog. Gene 197:47-64.
22. Harris, C. E., J. C. Biggs, A. J. Concannon, and A. J. Dodds. 1990. Peripheral blood and bone marrow findings in patients with acquired immune deficiency syndrome. Pathology 22:206-211.
23. Hill, P. J., A. Cockayne, P. Landers, J. A. Morrissey, C. M. Sims, and P. Williams. 1998. SirR, a novel iron-dependent repressor in Staphylococcus epidermidis. Infect. Immun. 66:4123-4129.
24. Homuth, M., P. Valentin-Weigand, M. Rohde, and G. F. Gerlach. 1998. Identification and characterization of a novel extracellular ferric reductase from Mycobacterium paratuberculosis. Infect. Immun. 66:710-716.
25. Hough, E., and D. Rogers. 1974. Crystal structure of ferrimycobactin P, a growth factor for the mycobacteria. Biochem. Biophys. Res. Commun. 57: 73-77.
26. Hu, J., and M. J. Miller. 1997. Total synthesis of a mycobactin S, a siderophore and growth promoter of Mycobacterium smegmatis, and determination of its growth inhibitory activity against Mycobacterium tuberculosis. J. Am. Chem. Soc. 119:3462-3468.
27. Hudson, A. T., and R. Bentley. 1970. Utilization of shikimic acid for the formation of mycobactin S and salicyclic acid by Mycobacterium smegmatis. Biochemistry 9:3984-3987.
28. Hudson, A. T., I. M. Campbell, and R. Bentley. 1970. Biosynthesis of 6-methylsalicylic acid by Mycobacterium phlei. Biochemistry 9:3988-3992.
29. Immanuel, C., G. S. Acharyulu, M. Kannapiran, R. Segaran, and G. R. Sarma. 1990. Acute phase proteins in tuberculous patients. Indian J. Chest Dis. Allied Sci. 32:15-23.
30. Inglis, N. F., K. Stevenson, A. H. Hosie, and J. M. Sharp. 1994. Complete sequence of the gene encoding the bacterioferritin subunit of Mycobacterium avium subspecies silvaticum. Gene 150:205-206.
31. Kikuchi, S., M. Fukumoto, and H. Takahashi. 1994. Iron storage in Mycobacterium smegmatis grown under iron-sufficient and iron-overload conditions. Biosci. Biotechnol. Biochem. 58:885-888.
32. Kochan, I. 1973. The role of iron in bacterial infections, with special consideration of host-tubercle bacillus interaction. Curr. Top. Microbiol. Immunol. 60:1-30.
33. Kochan, I., K. Ishak, M. Said, and J. Stotts. 1963. Study on the tuberculostatic factor of mammalian serum. Am. Rev. Respir. Dis. 88:818-826.
34. Kochan, I., C. Patton, and K. Ishak. 1963. Tuberculostatic activity of normal sera. J. Immunol. 90:711-719.
35. Kontoghiorghes, G. J., and E. D. Weinberg. 1995. Iron: mammalian defense systems, mechanisms of disease, and chelation therapy approaches. Blood Rev. 9:33-45.
36. Lane, S. J., P. S. Marshall, R. J. Upton, and C. Ratledge. 1998. Isolation and characterization of carboxymycobactins as the second extracellular siderophores in Mycobacterium smegmatis. BioMetals 11:13-20.
37. Lane, S. J., P. S. Marshall, R. J. Upton, C. Ratledge, and M. Ewing. 1995. Novel extracellular mycobactins, the carboxymycobactins from Mycobacterium avium. Tetrahedron Lett. 36:4129-4132.
38. Leite, C. Q. F., A. M. W. Barreto, and S. R. A. Leite. 1995. Thin-layer chromatography of mycobactins and mycolic acids for the identification of clinical mycobacteria. Rev. Microbiol. 26:192-199.
39. Lundrigan, M. D., J. E. L. Arceneaux, W. Zhu, and B. R. Byers. 1997. Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis. BioMetals 10:215-225.
40. MacCordick, H. J. 1985. Restrictive spatial modeling in structure and stability concepts of metallo-mycobactins. Nouv. J. Chim. 9:535-538.
41. MacCordick, H. J., J. J. Schleiffer, and G. Duplatre. 1985. Radiochemical studies of iron binding and stability in ferrimycobactin S. Radiochim. Acta 38:43-47.
42. Macham, L. P., and C. Ratledge. 1975. New group of water-soluble iron-binding compounds from mycobacteria. Exochelins. J. Gen. Microbiol. 89: 379-382.
43. Macham, L. P., C. Ratledge, and J. C. Nocton. 1975. Extracellular iron acquisition by mycobacteria: role of the exochelins and evidence against the participation of mycobactin. Infect. Immun. 12:1242-1251.
44. Marahiel, M. A., T. Stachelhaus, and H. D. Mootz. 1997. Modular peptide synthetases involved in non-ribosomal peptide synthesis. Chem. Rev. 97: 2651-2673.
45. Marshall, B. J., and C. Ratledge. 1972. Salicylic acid biosynthesis and its control in Mycobacterium smegmatis. Biochim. Biophys. Acta 264:106-116.
46. Matzanke, B. F., R. Boehnke, U. Moellmann, R. Reissbrodt, V. Schuenemann, and A. X. Trautwein. 1997. Iron uptake and intracellular metal transfer in mycobacteria mediated by xenosiderophores. BioMetals 10:193-203.
47. Matzanke, B. F., U. Mollmann, R. Reissbrodt, V. Schunemann, and A. X. Trautwein. 1998. Siderophore transport in mycobacteria analyzed by Mössbauer spectroscopy: possible routes to novel antibiotics against these organisms? Hyperfine Interact. 112:123-128.
48. McCready, K. A., and C. Ratledge. 1978. Amounts of iron, heme and related compounds in Mycobacterium smegmatis grown in various concentrations of iron. Biochem. Soc. Trans. 6:421-423.
49. McCullough, W. G., and R. S. Merkal. 1982. Structure of mycobactin J. Curr. Microbiol. 7:337-341.
50. Messenger, A. J. M., R. M. Hall, and C. Ratledge. 1986. Iron uptake processes in Mycobacterium vaccae R877R, a mycobacterium lacking mycobactin. J. Gen. Microbiol. 132:845-852.
51. Messenger, A. J. M., and C. Ratledge. 1982. Iron transport in Mycobacterium smegmatis: uptake of iron from ferric citrate. J. Bacteriol. 149:131-135.
52. Moyo, V. M., I. T. Gangaidzo, V. R. Gordeuk, C. F. Kiire, and A. P. Macphail. 1997. Tuberculosis and iron overload in Africa: a review. Cent. Afr. J. Med. 43:334-339.
53. Murakami, Y., S. Kato, M. Nakajima, M. Matsuoka, H. Kawai, K. Shin-Ya, and H. Seto. 1996. Formobactin, a novel free radical scavenging and neuronal cell protecting substance from Nocardia sp. J. Antibiot. 49:839-845.
54. Murray, M. J., A. B. Murray, M. B. Murray, and C. J. Murray. 1978. The adverse effect of iron repletion on the course of certain infections. Br. Med. J. 2:1113-1115.
55. Pessolani, M. C. V., D. R. Smith, B. Rivoire, J. McCormick, S. A. Hefta, S. T. Cole, and P. J. Brennan. 1994. Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae. J. Exp. Med. 180:319-327.
56. Quadri, L. E., J. Sello, T. A. Keating, P. H. Weinreb, and C. T. Walsh. 1998. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5:631-645.
57. Raghu, B., G. R. Sarma, and P. Venkatesan. 1994. Effect of haptoglobin on hemoglobin-supported growth and siderophore production of mycobacteria. Med. Sci. Res. 22:99-100.
58. Raghu, B., G. R. Sarma, and P. Venkatesan. 1993. Effect of iron on the growth and siderophore production of mycobacteria. Biochem. Mol. Biol. Int. 31:341-348.
59. Ratledge, C. 1984. Metabolism of iron and other metals by mycobacteria. Microbiol. Ser. 15:603-627.
60. Ratledge, C. 1982. Nutrition, growth and metabolism, p. 185-271. In C. Ratledge and J. Stanford (ed.), The biology of the mycobacteria, vol. 1. Academic Press Limited, San Diego, Calif.
61. Ratledge, C., and D. F. Ewing. 1978. The separation of the mycobactins from Mycobacterium smegmatis by using high-pressure liquid chromatography. Biochem. J. 175:853-857.
62. Ratledge, C., and M. J. Hall. 1972. Isolation and properties of auxotrophic mutants of Mycobacterium smegmatis requiring either salicylic acid or mycobactin. J. Gen. Microbiol. 72:143-150.
63. Ratledge, C., and M. J. Hall. 1970. Uptake of salicylic acid into mycobactin S by growing cells of Mycobacterium smegmatis. FEBS Microbiol. Lett. 10: 309-312.
64. Ratledge, C., and B. J. Marshall. 1972. Iron transport in Mycobacterium smegmatis. Role of mycobactin. Biochim. Biophys. Acta 279:58-74.
65. Ratledge, C., and P. V. Patel. 1976. Lipid-soluble, iron-binding compounds in Nocardia and related organisms, p. 372-385. In M. Goodfellow, G. H. Brownell, and J. A. Serrano (ed.), The biology of the Nocardiae. Academic Press, London, England.
66. Reimmann, C., L. Serino, M. Beyeler, and D. Haas. 1998. Dihydroaeruginoic acid synthetase and pyochelin synthetase, products of the pchEF genes, are induced by extracellular pyochelin in Pseudomonas aeruginosa. Microbiology 144:3135-3148.
67. Rusnak, F., W. S. Faraci, and C. T. Walsh. 1989. Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. Biochemistry 28:6827-6835.
68. Schmitt, M. P., M. Predich, L. Doukhan, I. Smith, and R. K. Holmes. 1995. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin represser (DtxR) from Corynebacterium diphtheriae. Infect. Immun. 63:4284-4289.
69. Serino, L., C. Reimmann, H. Baur, M. Beyeler, P. Visca, and D. Haas. 1995. Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa. Mol. Gen. Genet. 249:217-228.
70. Sharman, G. J., D. H. Williams, D. F. Ewing, and C. Ratledge. 1995. Determination of the structure of exochelin MN, the extracellular siderophore from Mycobacterium neoaurum. Chem. Biol. 2:553-561.
71. Sharman, G. J., D. H. Williams, D. F. Ewing, and C. Ratledge. 1995. Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis. Biochem. J. 305:187-196.
72. Sherman, D. R., P. J. Sabo, M. J. Hickey, T. M. Arain, G. G. Mahairas, Y. Yuan, C. E. Barry III, and C. K. Stover. 1995. Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria. Proc. Natl. Acad. Sci. USA 92:6625-6629.
73. Snow, G. A. 1970. Mycobactins: iron-chelating growth factors from mycobacteria. Bacteriol. Rev. 34:99-125.
74. Snow, G. A. 1965. The structure of mycobactin P, a growth factor for Mycobacterium johnei, and the significance of its iron complex. Biochem. J. 94: 160-165.
75. Snow, G. A., and A. J. White. 1969. Chemical and biological properties of mycobactins isolated from various mycobacteria. Biochem. J. 115:1031-1045.
76. Snow, G. A., and A. J. White. 1969. Isolation of mycobactins from various mycobacteria. Biochem. J. 111:785-792.
77. Stephenson, M. C., and C. Ratledge. 1980. Specificity of exochelins for iron transport in three species of mycobacteria. J. Gen. Microbiol. 116:521-523.
78. Tateson, J. E. 1970. Early steps in the biosynthesis of mycobactins P and S. Biochem. J. 118:747-753.
79. 78a. TubercuList Web Server. 1999, copyright date. [Online.] Institut Pasteur, Paris, France. http://www.pasteur.fr/Bio/TubercuList/. [7 June 1999, last date accessed.]
80. Wheeler, P. R., and C. Ratledge. 1994. Metabolism of Mycobacterium tuberculosis, p. 353-385. In B. R. Bloom (ed.), Tuberculosis: pathogenesis, protection, and control. American Society for Microbiology, Washington, D.C.
81. Winder, F. G. 1982. Mode of action of antimycobacterial agents and associated aspects of the molecular biology of the mycobacteria, p. 353-438. In C. Ratledge and J. Standford (ed.), The biology of the mycobacteria, vol. 1. Academic Press, London, England.
82. Wong, D. K., J. Gobin, M. A. Horwitz, and B. W. Gibson. 1996. Characterization of exochelins of Mycobacterium avium: evidence for saturated and unsaturated and for acid and ester forms. J. Bacteriol. 178:6394-6398.
83. Wong, D. K., B.-Y. Lee, M. A. Horwitz, and B. W. Gibson. 1999. Identification of Fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect. Immun. 67:327-336.
84. Yu, S., E. Fiss, and W. R. Jacobs, Jr. 1998. Analysis of the exochelin locus in Mycobacterium smegmatis: biosynthesis genes have homology with genes of the peptide synthetase family. J. Bacteriol. 180:4676-4685.
85. Zhu, W., J. E. L. Arceneaux, M. L. Beggs, B. R. Byers, K. D. Eisenach, and M. D. Lundrigan. 1998. Exochelin genes in Mycobacterium smegmatis: identification of an ABC transporter and two non-ribosomal peptide synthetase genes. Mol. Microbiol. 29:629-639.
86. Zou, P., I. Borovok, D. Lucana, D. Muller, and H. Schrempf. 1999. The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS. Microbiology 145:549-559.