Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase

Nature

Volumn 406, Issue 6797, 2000, Pages 735-738

  McKinney, John D ^a,c,e   Höner Zu Bentrup, Kerstin ^b,c,f   Muñoz Elias, Ernesto J ^c   Miczak, Andras ^b,c,f   Chen, Bing ^a   Chan, Wal Tsing ^c   Swenson, Dana ^b,c,e   Sacchettini, James C ^d   Jacobs Jr , William R ^a   Russell, David G ^b,c  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c ROCKEFELLER UNIVERSITY   (United States)

^d TEXAS A AND M UNIVERSITY   (United States)

^e Department of Obstetrics Gynecology   (United States)

^f UNIVERSITY OF SZEGED   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

GLYOXYLIC ACID; ISOCITRATE LYASE;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; BACTERIAL GROWTH; BACTERIAL METABOLISM; BACTERIAL VIRULENCE; FATTY ACID METABOLISM; MACROPHAGE ACTIVATION; MOUSE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; TUBERCULOSIS;

ANIMALS; BACTERIAL PROTEINS; FATTY ACIDS; ISOCITRATE LYASE; LUNG; MACROPHAGE ACTIVATION; MACROPHAGES; MICE; MICE, INBRED BALB C; MICE, INBRED C57BL; MICE, KNOCKOUT; MUTAGENESIS; MYCOBACTERIUM TUBERCULOSIS; RECOMBINANT FUSION PROTEINS; TUBERCULOSIS; VIRULENCE;

ANIMALIA; BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0342794213     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35021074     Document Type: Article

References (31)

1. McKinney, J. D., Jacobs, W. R. & Bloom, B. R. in Emerging Infections (eds Krause, R., Gallin, J. I. & Fauci, A. S.) 51-146 (Academic, New York, 1998).
2. Parrish, N. M., Dick, J. D. & Bishai, W. R. Mechanisms of latency in Mycobacterium tuberculosis. Trends Microbiol. 6, 107-112 (1998).
3. Clark, D. P. & Cronan, J. E. Jr in Escherichia coli and Salmonella: Cellular and Molecular Biology (ed. Neidhardt, F. C.) 343-357 (ASM Press, Washington DC, 1996).
4. Cronan, J. E. Jr. & LaPorte, D. in Escherichia coli and Salmonella: Cellular and Molecular Biology (ed. Neidhardt, F. C.) 206-216 (ASM Press, Washington DC, 1996).
5. Segal, W. in The Mycobacteria: A Sourcebook (eds Kubica, G. P. & Wayne, L. G.) 547-573 (Dekker, New York, 1984).
6. Wheeler, P. R. & Ratledge, C. in Tuberculosis: Pathogenesis, Protection, and Control (ed. Bloom, B. R.) 353-385 (ASM Press, Washington DC, 1994).
7. Höner zu Bentrup, K., Miczak, A., Swenson, D. L. & Russell, D. G. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. J. Bacteriol. 181, 7161-7167 (1999).
8. Sturgill-Koszycki, S., Haddix, P. L. & Russell, D. G. The interaction between Mycobacterium and the macrophage analyzed by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 18, 2558-2565 (1997).
9. Graham, J. E. & Clark-Curtiss, J. E. Identification of Mycobacterium tuberculosis RNAs synthesized in response to phagocytosis by human macrophages by selective capture of transcribed sequences (SCOTS). Proc. Natl Acad. Sci. USA 96, 11554-11559 (1999).
10. Farewell, A., Diez, A. A., DiRusso, C. C. & Nystrom, T. Role of the Escherichia coli FadR regulator in stasis survival and growth phase-dependent expression of the uspA, fad, and fab genes. J. Bacteriol. 178, 6443-6450 (1996).
11. Spector, M. P. et al. The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of Salmonella typhimurium is a phase 1 starvation-stress response (SSR) locus. Microbiol. 145, 15-31 (1999).
12. Suryanarayana Murthy, P., Sirsi, M. & Ramakrishnan, T. Effect of age on the enzymes of tricarboxylic acid and related cycles in Mycobacterium tuberculosis H37Rv. Amer. Rev. Resp. Dis. 108, 689-690 (1973).
13. Wayne, L. G. & Lin, K. Y. Glyoxylate metabolism and adaptation of Mycobacterium tuberculosis to survival under anaerobic conditions. Infect. Immunol. 37, 1042-1049 (1982).
14. Rees, R. J. W. & Hart, P. D. Analysis of the host-parasite equilibrium in chronic murine tuberculosis by total and viable bacillary counts. Br. J. Exp. Pathol. 42, 83-88 (1961).
15. Wallace, J. G. The heat resistance of tubercle bacilli in the lungs of infected mice. Am. Rev. Respir. Dis. 83, 866-871 (1961).
16. Hart, P. D. & Young, M. R. Interference with normal phagosome-lysosome fusion in macrophages, using ingested yeast cells and suramin. Nature 256, 47-49 (1975).
17. Sturgill-Koszycki, S. et al. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 263, 678-681 (1994).
18. Sturgill-Koszycki, S., Schaible, U. E. & Russell, D. G. Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis. EMBO J. 15, 6960-6968 (1996).
19. Clemens, D. L. & Horwitz, M. A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J. Exp. Med. 184, 1349-1355 (1996).
20. James, P. E., Grinberg, O. Y., Michaels, G. & Swartz, H. M. Intraphagosomal oxygen in stimulated macrophages. J. Cell. Physiol. 163, 241-247 (1995).
21. Schaible, U. E., Sturgill-Koszycki, S., Schlesinger, P. H. & Russell, D. G. Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages. J. Immunol. 160, 1290-1296 (1998).
22. Via, L. E. et al. Effects of cytokines on mycobacterial phagosome maturation. J. Cell Sci. 111, 897-905 (1998).
23. Pelicic, V. et al. Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis. Proc Natl Acad Sci USA 94, 10955-10960 (1997).
24. Mitchison, D. A. Treatment of tuberculosis. The Mitchell lecture 1979. J. R. Coll. Physicians Lond. 14, 91-99 (1980).
25. Girling, D. J. in The Biology of the Mycobacteria, Volume 3: Clinical Aspects of Mycobacterial Disease (eds Ratledge, C., Stanford, J. & Grange, J. M.) 285-323 (Academic, London, 1989).
26. Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T. & Jacobs, W. R. Jr Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4, 1911-1919 (1990).
27. Stover, C. K. et al. New use of BCG for recombinant vaccines. Nature 351, 456-460 (1991).
28. Pavelka, M. S. & Jacobs, W. R. Comparison of the construction of unmarked deletion mutants in Mycobacterium smegmatis, Mycobacterium bovis bacillus Calmette-Guerin, and Mycobacterium tuberculosis H37Rv by allellic exchange. J. Bacteriol. 181, 4780-4789 (1999).
29. Cormack, B. P., Valdivia, R. H. & Falkow, S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173, 33-38 (1996).
30. Russo-Marie, F., Roederer, M., Sager, B., Herzenberg, L. A. & Kaiser, D. Beta-galactosidase activity in single differentiating bacterial cells. Proc Natl Acad Sci USA 90, 8194-8198 (1993).
31. Sharma, V. et al. The structure of isocitrate lyase from Mycobacterium tuberculosis: a lynchpin to persistence of infection. Nature Struct. Biol. (in the press).