Nutrient acquisition by mycobacteria

Microbiology

Volumn 154, Issue 3, 2008, Pages 679-692

  Niderweis, Michael ^a  

^a University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARBOHYDRATE; CATION; MEMBRANE PROTEIN; PHOSPHATE; PORIN; SULFATE; BACTERIAL PROTEIN; CARRIER PROTEIN;

BACTERIAL CELL; BACTERIAL GROWTH; BIOCHEMISTRY; CARBOHYDRATE TRANSPORT; CELL MEMBRANE; CYTOPLASM; GENOMICS; LIFESTYLE; LIPID TRANSPORT; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUTRIENT UPTAKE; NUTRITIONAL REQUIREMENT; PERMEABILITY BARRIER; PRIORITY JOURNAL; REVIEW; SOIL; SPECIES HABITAT; TUBERCULOSIS; COMPARATIVE STUDY; GENETICS; METABOLISM; PHYSIOLOGY; TRANSPORT AT THE CELLULAR LEVEL;

CORYNEBACTERINEAE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; CARRIER PROTEINS; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 42949135614     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2007/012872-0     Document Type: Review

References (121)

1. Agranoff, D. & Krishna, S. (2004). Metal ion transport and regulation in Mycobacterium tuberculosis. Front Biosci 9, 2996-3006.
2. Barry, C. E., III, Lee, R. E., Mdluli, K., Sampson, A. E., Schroeder, B. G., Slayden, R. A. & Yuan, Y. (1998). Mycolic acids: structure, biosythesis and physiological functions. Prog Lipid Res 37, 143-179.
3. Bell, A. W., Buckel, S. D., Groarke, J. M., Hope, J. N., Kingsley, D. H. & Hermodson. M. A. (1986). The nucleotide sequences of the rbsD. rbsA, and rbsC genes of Escherichia coli K12. J Biol Chem 261, 7652-7658.
4. Bentley, S. D., Chater, K. F., Cerdeno-Tarraga, A. M., Challis, G. L., Thomson, N. R., James, K. D., Harris, D. E., Quail, M. A., Kieser, H. & other authors (2002). Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417, 141-147.
5. Bertram, R., Schlicht, M., Mahr, K., Nothaft, H., Saier, M. H., Jr & Titgemeyer, F. (2004). In silico transcriptional analysis of carbohydrate uptake systems of Streptomyces coelicolor A3(2). J Bacteriol 186, 1362-1373.
6. Beveridge, T. J. (1995). The periplasmic space and the periplasm in Gram-positive and Gram-negative bacteria. ASM News 61, 125-130.
7. Beveridge, T. J. (1999). Structures of gram-negative cell walls and their derived membrane vesicles. J Bacteriol 181, 4725-4733.
8. Beveridge, T. J. & Kadurugamuwa, J. L. (1996). Periplasm, periplasmic spaces, and their relation to bacterial wall structure: novel secretion of selected periplasmic proteins from Pseudomonas aeruginosa. Microb Drug Resist 2, 1-8.
9. Bhatt, K., Banerjee, S. K. & Chakraborti, P. K. (2000). Evidence that phosphate specific transporter is amplified in a fluoroquinolone resistant Mycobacterium smegmatis. Eur J Biochem 267, 4028-4032.
10. Borich, S. M., Murray, A. & Gormley, E. (2000). Genomic arrangement of a putative operon involved in maltose transport in the Mycobacterium tuberculosis complex and Mycobacterium leprae. Microbios 102, 7-15.
11. Braibant, M., Lefevre, P., de Wit, L., Peirs, P., Ooms, J., Huygen, K., Andersen, A. B. & Content, J. (1996). A Mycobacterium tuberculosis gene cluster encoding proteins of a phosphate transporter homologous to the Escherichia coli Pst system. Gene 176, 171-176.
12. Braibant, M., Gilot, P. & Content, J. (2000). The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol Rev 24, 449-467.
13. Braun, V. & Killmann, H. (1999). Bacterial solutions to the iron-supply problem. Trends Biochem Sci 24, 104-109.
14. Brennan, P. J. & Nikaido, H. (1995). The envelope of mycobacteria. Annu Rev Biochem 64, 29-63.
15. Brinkkötter, A., Kloss, H., Alpert, C. & Lengeler, J. W. (2000). Pathways for the utilization of N-acetylgalactosamine and galactosamine in Escherichia coli. Mol Microbiol 37, 125-135.
16. Chakrabarti, A. C. & Deamer, D. W. (1992). Permeability of lipid bilayers to amino acids and phosphate. Biochim Biophys Acta 1111, 171-177.
17. Chan, E. D., Chan, J. & Schluger, N. W. (2001). What is the role of nitric oxide in murine and human host defense against tuberculosis? Current knowledge. Am J Respir Cell Mol Biol 25, 606-612.
18. Clegg, S., Yu, F., Griffiths, L. & Cole, J. A. (2002). The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K-12: two nitrate and three nitrite transporters. Mol Microbiol 44, 143-155.
19. Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S. & other authors (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete geenome sequence. Nature 393, 537-544.
20. Content, J., Braibant, M., Connell, N. & Ainsa, J. A. (2005). Transport Processes. In Tuberculosis and the Tubercle Bacillus, pp. 379-401. Edited by S. Cole, K. D. Eisenach, D. N. McMurray & W. R. Jacobs. Washington, DC: ASM Press.
21. Cox, R. A. & Cook, G. M. (2007). Growth regulation in the mycobacterial cell. Curr Mol Med 7, 231-245.
22. Daffé, M. & Draper, P. (1998). The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol 39, 131-203.
23. Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D. & von Heijne, G. (2005). Global topology analysis of the Escherichia coli Inner membrane proteome. Science 308, 1321-1323.
24. Dirusso, C. C. & Black, P. N. (2004). Bacterial long chain fatty acid transport: gateway to a fatty acid-responsive signalling system. J Biol Chem 279, 49563-49566.
25. Draper, P. (1998). The outer parts of the mycobacterial envelope as permeability barriers. Front Biosci 3, D1253-D1261.
26. Dubnau, E., Chan, J., Mohan, V. P. & Smith. I. (2005). Responses of Mycobacterium tuberculosis to growth in the mouse lung. Infect Immun 73, 3754-3757.
27. Dumas, F., Koebnik, R., Winterhalter, M. & van Gelder, P. (2000). Sugar transport through maltoporin of Escherichia coli. Role of polar tracks. J Biol Chem 275, 19747-19751.
28. Edson, N. L. (1951). The intermediary metabolism of the mycobacteria. Bacteriol Rev 15, 147-182.
29. Eriksson, S., Lucchini, S., Thompson, A., Rhen, M. & Hinton, J. C. (2003). Unravelling the biology of macropage infection by gene expression profiling of intracellular Salmonella enterica. Mol Microbiol 47, 103-118.
30. 2155: is there a clue for the unique transformability of the strain? Microbiology 151, 2075-2086.
31. Eze, M. O. & McElhaney, R. N. (1981). The effect of alterations in the fluidity and phase state of the membrane lipids on the passive permeation and facilitated diffusion of glycerol in Escherichia coli. J Gen Microbiol 124, 299-307.
32. Faller, M., Niederweis, M. & Schulz, G. E. (2004). The structure of a mycobacterial outer-membrane channel. Science 303, 1189-1192.
33. Franke, W. & Schillinger, A. (1944). Zum Stoffwechsel der saeurefesten Bakterien. I. Orientierende aerobe Reihenversuche. Biochem Z 319, 313-334 (in German).
34. Gebhard, S., Tran, S. L. & Cook, G. M. (2006). The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate. Microbiology 152, 3453-3465.
35. Graham, L. L., Beveridge, T. J. & Nanninga, N. (1991). Periplasmic space and the concept of the periplasm. Trends Biochem Sci 16, 328-329.
36. Gutknecht, R., Beutler, R., Garcia-Alles, L. F., Baumann, U. & Erni, B. (2001). The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J 20, 2480-2486.
37. Hancock, R. E., Farmer, S. W., Li, Z. S. & Poole, K. (1991). Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli. Antimicrob Agent Chemother 351, 1309-1314.
38. Hoffmann, C., Leis, L., Niederweis, MI., Plitzko, J. M. & Engelhardt, H. (2008). Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci U S A (in press).
39. Izumori, K., Yamanaka, K. & Elbein, D. (1976). Pentose metabolism in Mycobacterium smegmatis: specificity of induction of pentose isomerases. J Bacteria, 128, 587-591.
40. Jackson, M., Stadthagen, G. & Gicquel, B. (2007). Long-chain multiple meethyl -branched la tty acid-containing lipids of Mycobacterium tuberculosis: biosynthesis, transport, regulation and biological activities. Tuberculosis 87, 78-86.
41. Jarlier, V. & Nikaido, H. (1990). Permeability barrier to hydrophilic solutes in Mycobacterium chelonei. J Bacteriol 172, 1418-1423.
42. Jia, W. & Cole, J. A. (2005). Nitrate and nitrite transport in Escherichia coli. Biochem Soc Trans 33, 159-161.
43. Kana, B. D. & Mizrahi, V. (2004). Molecular genetics of Mycobacterium tuberculosis in relation to the discovery of novel drugs and vaccines. Tuberculosis 84, 63-75.
44. Kartmann, B., Stenger, S. & Niederweis, M. (1999). Porins in the cell wall of Mycobacterium tuberculosis. J Bacteriol 181, 6543-6546. (Authors' correction in J Bacteriol 181, 7650)
45. Koch, R. (1882). Die Aetiologie der Tuberculose. Berliner Klinische Wochenzeitschrift 19, 18 (in German).
46. Koebnik, R., Locher, K. P. & van Gelder, P. (2000). Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37, 239-253.
47. Lichtinger, T., Heym, B., Maier E, Eichner, H., Cole, S. T. & Benz, R. (1999). Evidence for a small anion -selective channel in the cell wall of Mycobacterium bovis BCG besides a wide cation-selective pore. FEBS Lett 454, 349-355.
48. Liu, J., Rosenberg, E. Y. & Nikaido, H. (1995). Fluidity of the lipid domain of cell wall from Myrobacterium chelonae. Proc Natl Acad Sci U S A 92, 11254-11258.
49. Liu, J., Barry, C. E., III, Besra, G. S. & Nikaido, H. (1996). Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J Biol Chem 271, 29545-29551.
50. Machowski, E. E., Dawes, S. & Mizrahi, V. (2005). TB tools to tell the tale - molecular genetic methods for mycobacterial research. Int J Biochem Cell Biol 37, 54-68.
51. Mahfoud, M., Sukumaran, S., Hülsmann, P., Grieger, K. & Niederweis, M. (2006). Topology of the porin MspA in the outer membrane of Mycobacterium smegmatis. J Biol Chem 281, 5908-5915.
52. Maier, C., Bremer, E., Schmid, A. & Benz, R. (1988). Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site. J Biol Chem 263, 2493-2499.
53. Matias, V. R. & Beveridge, T. J. (2005). Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol Microbiol 56, 240-251.
54. Matias, V. R. & Beveridge, T. J. (2006). Native cell wall organization shown by cryo-electron microscopy confirms the existence of a perisplasmic pace in Staphylococcus aureus. J Bacteriol 188, 1011-1021.
55. Matias, V. R., Al-Amoudi, A., Dubochet, J. & Beveridge, T. J. (2003). Cryo-transmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa. J Bacteriol 185, 6112-6118.
56. McAdam, R. A., Weisbrod, T. R., Martin, J., Scuderi, J. D., Brown, A. M., Cirillo, J. D., Bloom, B. R. & Jacobs, W. R., Jr (1995). In vivo growth characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis. Infect Immun, 63, 1004-1012.
57. McKinney, J. D., Honer zu Bentrup, K., Munoz-Elias, E. J., Miczak, A., Chen, B., Chan, W. T., Swenson, D., Sacchettini, J. C., Jacobs, W. R., Jr & Russell, D. G. (2000). Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 406, 735-738.
58. Mills, C. D. (2001). Macrophage arginine metabolism to ornithine/ urea or nitric oxide/citrulline: a life or death issue. Crit Rev Immunol 21, 399-425.
59. Mineda, T., Ohara, N., Yukitake, H. & Yamada, T. (1998). The ribosomes contents of mycobacteria. New Microbiol 21, 1-7.
60. Minnikin, D. E. (1982). Lipids: complex lipids, their chemistry, biosynthesis and roles. In The Biology of the Mycobacteria: Physiology, Identification and Clussification, pp. 95-184. Edited by C. Ratledge & J. Stanford. London: Academic Press.
61. Moir, J. W. & Wood, N. J. (2001). Nitrate and nitrite transport in bacteria. Cell Mol Life Sci 58, 215-224.
62. Molle, V., Saint, N., Campagna, S., Kremer, L., Lea, E., Draper, P. & Molle, G. (2006). pH-dependent pore-forming activity of OmpATb from Mycobacterium tuberculosis and characterization of the channel by peptidic dissection. Mol Microbiol 61, 826-837.
63. Munoz-Elias, E. J. & McKinney, J. D. (2005). Mycobacterium tuberculosis isocitrate iyases 1 and 2 are jointly required for in vivo growth and virulence. Nat Med 11, 638-644.
64. Murphy, H. N., Stewart, G. R., Mischenko, V. V., Apt, A. S., Harris, R., McAlister, M. S., Driscoll, P. C., Young, D. B. & Robertson, B. D. (2005). The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis. J Biol Chem 280, 14524-14529.
65. Nathan, C. & Shiloh, M. U. (2000). Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc Natl Acad Sci U S A 97, 8841-8848.
66. Neyrolles, O., Hernandez-Pando, R., Pietri-Rouxel, F., Pietri-Rouxel, F., Fornes, P., Tailleux, L., Barrios Payan, J. A., Pivert E., Bordat Y., Aguilar, D. & other authors (2006). Is adipose tissue a place for Mycobacterium tuberculosis persistence PLoS ONE 1, e43.
67. Niederweis, M. (2003). Mycobacterial porins - new channel proteins in unique outer membranes. Mol Nlicrobiol 49, 1167-1177.
68. Niederweis, M., Ehrt, S., Heinz, C., Klöcker, U., Karosi, S., Swiderek, K. M., Riley, L. W. & Benz, R. (1999). Cloning of the mspA, gene encoding a porin from Mycobacterium smeqmatis. Mol Microbiol 33, 933-945.
69. Nikaido, H. (1994). Porins and specific diffusion channels in bacterial outer membranes. J Biol Chem 269, 3905-3908.
70. Nikaido, H. (2003). Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67, 593-656.
71. Nikaido, H., Rosenberg, E. Y. & Foulds, J. (1983). Porin channels in Escherichia coli: studies with beta-lactams in intact cells. J Bacteriol 153, 232-240.
72. Nikaido, H., Kim, S. H. & Rosenberg, E. Y. (1993). Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol Microbiol 8, 1025-1030.
73. Nolden, L., Ngouoto-Nkili, C. E., Bendt, A. K., Kramer, R. & Burkovski, A. (2001). Sensing nitrogen limitation in Corynebacterium glutamicum: the role of glnK and glnD. Mol Microbiol 42, 1281-1295.
74. Nothaft, H., Dresel, D., Willimek, A., Mahr, K., Niederweis, M. & Titgemeyer, F. (2003). The phosphotransferase system of Streptomyces coelicolor is biased for N-acetylglucosamine metabolism. J Bacteriol 185, 7019-7023.
75. Ohno, H., Zhu, G., Mohan, V. P., Chu, D., Kohno, S., Jacobs, W. R., Jr & Chan, J. (2003). The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol 5, 637-648.
76. Paul, T. R. & Beveridge, T. J. (1992). Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols. J Bacteriol 174, 6508-6517.
77. Paul, T. R. & Beveridge, T. J. (1994). Preservation of surface lipids and determination of ultrastructure of Mycobacterium kansasii by freeze-substitution. Infect Immun 62, 1542-1550.
78. Paula, S., Volkov, A. G., Van Hoek, A. N., Haines, T. H. & Deamer. D. W. (1996). Permeation of protons, potassium ions, and small polar molecules through phospholipid bilayers as a function of membrane thickness. Biophys J 70, 339-348.
79. Peirs, P., Lefevre, P., Boarbi, S., Wang, X. M., Denis, O., Braibant, M., Pethe, K., Locht, C., Huygen, K. & Content, J. (2005). Mycobacterium tuberculosis with disruption in genes encoding the phosphate binding proteins PstS1 and PstS2 is deficient in phosphate uptake and demonstrates reduced in vivo virulence. Infect Immun 73, 1898-1902.
80. Ramakrishnan, T., Murthy, P. S. & Gopinathan, K. P. (1972). Intermediary metabolism of mycobacteria. Bacteriol Rev 36, 65-108.
81. Ratledge, C. (1982). Nutrition, growth and metabolism. In The Biology of the Mycobacteria, pp. 186-212. Edited by C. Ratledge & J. Stanford. London: Academic Press.
82. Ratledge, C. & Dover, L. G. (2000). Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 54, 881-941.
83. Raynaud, C., Guilhot, C., Rauzier, J., Bordat, Y., Pelicic, V., Manganelli, R., Smith, I., Gicquel, B. & Jackson, M. (2002a). Phospholipases C are involved in the virulence of Mycobacterium tuberculosis. Mol Microbiol 45, 203-217.
84. Raynaud, C., Papavinasasundaram, K. G., Speight R. A., Springer. B., Sander, P., Böttger, E. C., Colston, M. J. & Draper, P. (2002b). The functions of OmpATb, a pore-forming protein of Mycobacterium tuberculosis. Mol Microbiol 46, 191-201.
85. Rengarajan, J., Bloom, B. R. & Rubin, E. J. (2005). Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc Natl Acad Sci U S A 102, 8327-8332.
86. Rimmele, M. & Boos, W. (1994). Trehalose-6-phosphate hydrolase of Escherichia coli. J Bacteriol 176, 5654-5664.
87. Rodriguez, G. M. (2006). Control of iron metabolism in Mycobacterium tuberculosis. Trends Microbiol 14, 320-327.
88. Rodriguez, G. M. & Smith, I. (2006). Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J Bacteriol 188, 424-430.
89. Rowe, J. J., Ubbink-Kok, T., Molenaar, D., Konings, W. N. & Driessen, A. J. (1994). NarK is a nitrite-extrusion system involved in anaerobic nitrate respiration by Escherichia coli. Mol Microbiol 12, 579-586.
90. Russell, D. G. (2003). Phagosomes, fatty acids and tuberculosis. Nat Cell Biol 5, 776-778.
91. Sa-Nogueira, I., Nogueira, T. V., Soares, S. & de Lencastre, H. (1997). The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression. Microbiology 143, 957-969.
92. Sassetti, C. M. & Rubin, E. J. (2003). Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci U S A 100, 12989-12994.
93. Schnappinger, D., Ehrt, S., Voskuil, M. I., Liu, Y., Mangan, J. A., Monahan, I. M., Dolganov, G., Efron, B., Butcher, P. D. & other authors (2003). Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J Exp Med 198, 693-704.
94. Schönert, S., Buder, T. & Dahl, M. K. (1999). Properties of maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) in Bacillus subtilis: evidence for its contribution to maltodextrin utilization. Res Microbiol 150, 167-177.
95. Senaratne, R. H., Mobasheri, H., Papavinasasundram, K. G., Jenner, P., Lea, E. J. & Draper, P. (1998). Expression of a gene for a porin-like of the OmpA family from Mycobacterium tuberculosis H37Rv. J Bacteriol 180, 3541-3547.
96. Seth, A. & Connell, N. D. (2000), Amino acid transport and metabolism in mycobacteria: cloning, interruption, and characterization of an L-Arginine/gamma-aminobutyric acid permease in Mycobacterium bovis BCG. J Bacteriol 182, 919-927.
97. Sohaskey, C. D. (2005). Regulation of nitrate reductase activity in Mycobacterium tuberculosis by oxygen and nitric oxide. Microbiology 151, 3803-3810.
98. Sohaskey, C. D. & Wayne, L. G. (2003). Role of narK2X and narGHJI in hypoxic upregulation of nitrate reduction by Mycobacterium tuberculosis. J. Bacteriol 185, 7247-7256.
99. Sørensen, K. I. & Hove-Jensen, B. (1996). Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression. J Bacteriol 178, 1003-1011.
100. Stahl, C., Kubetzko, S., Kaps, I., Seeber, S., Engelhardt, H. & Niederweis, M. (2001). MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis. Mol Microbiol 40, 451-464. (Authors' correction in Mol Microbiol 457, 1509)
101. Stephan, J., Bender, J., Wolschendorf, F., Hoffmann, C., Roth, E., Mailänder, C., Engelhardt, H. & Niederweis, M. (2005). The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients. Mol Microbiol 58, 714-730.
102. Sumiya, M., Davis, E. O., Packman, L. C., McDonald, T. P. & Henderson, P. J. (1995). Molecular genetics of a receptor protein for D-xylose, encoded by the gene xylF, in Escherichia coli. Receptors Channels 3, 117-128.
103. Talaue, M. T., Venketaraman, V., Hazbon, M. H., Peteroy-Kelly, M., Seth, A., Colangeli, R., Alland, D. & Connell, N. D. (2006). Arginine homeostatis in J774.1 macrophages in the context of Mycobacterium bovis BCG infection. J Bacteriol 188, 4830-4840.
104. Timm, J., Post, F. A., Bekker, L. G., Walther, G. B., Wainwright, H. C.; Manganelli, R., Chan, W. T., Tsenova, L., Gold, B. & other authors (2003). Differential expression of iron-, carbon-, and oxygen-responsive mycobacterial genes in the lungs of chronically infected mice and tuberculosis patients. Proc Natl Acad Sci U S A 100, 14321-14326.
105. Titgemeyer, F., Amon, J., Parche, S., Mahfoud, M., Ball, J., Schlicht, M., Rehm, N., Hillmann, D., Stephan, J. & other authors (2007). A genomic view of sugar transport in Mycobacterium smegmatis and Mycobacterium tuberculosis. J. Bacteriol 189, 5903-5915.
106. Trivedi, O. A., Arora, P., Sridharan, V., Tickoo, R., Mohanty, D. & Gokhale, R. S. (2004). Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428, 441-445.
107. Ulrichs, T. & Kaufmann, S. H. (2006). New insights into the function of granulomas in human tuberculosis. J Pathol 208, 261-269.
108. van Veen, H. W. (1997). Phosphate transport in prokaryotes: molecules, mediators and mechanisms. Antonie Van Leeuwenhoek 72, 299-315.
109. van Wezel, G. P., Mahr, K., Konig, M., Traag, B. A., Pimentel-Schmitt, E. F., Willimek, A. & Titgemeyer, F. (2005). GlcP constitutes the major glucose uptake system of Streptomyces coelicolor A3(2). Mol Microbiol 55, 624-636.
110. Voskuil, M. I., Schnappinger, D., Visconti, K. C., Harrell, M. I., Dolganov, G. M., Sherman, D. R. & Schoolnik, G. K. (2003). Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J Exp Med 198, 705-713.
111. Vyas, N. K., Vyas, M. N. & Quiocho, F. A. (2003). Crystal structure of M. tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions. Structure 11, 765-774.
112. Webb, M. R. (2003). Mycobacterial ABC transport system: structure of the primary phosphate receptor. Structure 11, 736-738.
113. Wheeler, P. R., Bulmer, K. & Ratledge, C. (1990). Enzymes for biosynthesis de novo and elongation of fatty acids in mycobacteria grown in host cells: is Mycobacterium leprae competent in fatty acid biosynthesis? J Gen Microbiol 136, 211-217.
114. Wolschendorf, F., Mahfoud, M. & Niederweis, M. (2007). Porins are required for uptake of phosphates by Mycobacterium smegmatis. J Bacteriol 189, 2435-2442.
115. Wood, K. V. (1995). Marker proteins for gene expression. Curr Opin Biotechnol 6, 50-58.
116. Woodruff, P. J., Carlson, B. L., Siridechadilok, B., Pratt, M. R., Senaratne, R. H., Mougous, J. D., Riley, L. W., Williams, S. J. & Berozzi, C. R. (2004). Trchalose is required for growth of Mycobacterium smegmatis. J Biol Chem 279, 28835-28843.
117. Woodson. K. & Devine. K. M. (1994). Analysis of a ribose transport operon from Bacillus subtilis. Microbiology 140, 1829-1838.
118. Wooff, E., Michell, S. L., Gordon, S. V., Chambers, M. A., Bardarov, S., Jacobs, W. R., Jr, Hewinson, R. G. & Wheeler, P. R. (2002). Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Mol Microbiol 43, 653-663.
119. Yabu, K. (1967). The uptake of D-glutamic acid by Mycobacterium avium. Biochim Biophys Acta 135, 181-183.
120. Yabu, K. (1971). Amino acid transport in Mycobacterium smegmatis. J Bacteriol 102, 6-13.
121. Yabu, K. (1971). Aspartic acid transport in Mycobacterium smegmatis. Jpn J Microbiol 15, 449-456.