Role of protein kinase G in growth and glutamine metabolism of Mycobacterium bovis BCG

Journal of Bacteriology

Volumn 187, Issue 16, 2005, Pages 5852-5856

  Nguyen, Liem ^a,c   Walburger, Anne ^a,d   Houben, Edith ^a   Koul, Anil ^b,e   Muller, Stefan ^b   Morbitzer, Monika ^b   Klebl, Bert ^b   Ferrari, Giorgio ^a,f   Pieters, Jean ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b Axxima Pharmaceuticals AG   (Germany)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^d CENTRE D IMMUNOLOGIE DE MARSEILLE LUMINY   (France)

^e JANSSEN RESEARCH FOUNDATION   (Belgium)

^f ACTELION PHARMACEUTICALS LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC GMP DEPENDENT PROTEIN KINASE; GLUTAMINE; PROTEIN SERINE THREONINE KINASE;

AMINO ACID METABOLISM; AMINO ACID TRANSPORT; ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL METABOLISM; BACTERIAL STRAIN; BACTERIAL SURVIVAL; CYTOSOL; ENZYME ACTIVITY; ENZYME SPECIFICITY; EUKARYOTE; GENE DELETION; GLNH GENE; LYSOSOME; MACROPHAGE; MYCOBACTERIUM BOVIS; NONHUMAN; OPERON; PHAGOSOME; PKNG GENE; PRIORITY JOURNAL;

CYCLIC GMP-DEPENDENT PROTEIN KINASES; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTAMINE; MYCOBACTERIUM BOVIS; TRANSCRIPTION, GENETIC; TRITIUM;

CORYNEBACTERINEAE; EUKARYOTA; MYCOBACTERIUM BOVIS BCG;

EID: 23644458298     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.16.5852-5856.2005     Document Type: Article

References (19)

1. Av-Gay, Y., and M. Everett. 2000. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 8:238-244.
2. Bidlingmeyer, B. A., S. A. Cohen, and T. L. Tarvin. 1984. Rapid analysis of amino acids using pre-column derivatization. J. Chromatogr. 336:93-104.
3. Bidlingmeyer, B. A., S. A. Cohen, T. L. Tarvin, and B. Frost. 1987. A new, rapid, high-sensitivity analysis of amino acids in food type samples. J Assoc. Off. Anal. Chem. 70:241-247.
4. Braibant, M., P. Gilot, and J. Content. 2000. The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol. Rev. 24:449-467.
5. Chang, J. Y., and R. Knecht. 1991. Direct analysis of the disulfide content of proteins: methods for monitoring the stability and refolding process of cystine-containing proteins. Anal. Biochem. 197:52-58.
6. Cole, S. T. 1999. Learning from the genome sequence of Mycobacterium tuberculosis H37Rv. FEBS Lett. 452:7-10.
7. 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, B. G. Barrell, et al. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
8. Cowley, S., M. Ko, N. Pick, R. Chow, K. J. Downing, B. G. Gordhan, J. C. Betts, V. Mizrahi, D. A. Smith, R. W. Stokes, and Y. Av-Gay. 2004. The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo. Mol. Microbiol. 52:1691-1702.
9. Gatfield, J., and J. Pieters. 2003. Molecular mechanisms of host-pathogen interaction: entry and survival of mycobacteria in macrophages. Adv. Immunol. 81:45-96.
10. Harth, G., D. L. Clemens, and M. A. Horwitz. 1994. Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity. Proc. Natl. Acad. Sci. USA 91:9342-9346.
11. Harth, G., and M. A. Horwitz. 1999. An inhibitor of exported Mycobacterium tuberculosis glutamine synthetase selectively blocks the growth of pathogenic mycobacteria in axenic culture and in human monocytes: extracellular proteins as potential novel drug targets. J. Exp. Med. 189:1425-1436.
12. Harth, G., P. C. Zamecnik, J. Y. Tang, D. Tabatadze, and M. A. Horwitz. 2000. Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to glutamine synthetase mRNA inhibits glutamine synthetase activity, formation of the poly-L-glutamate/glutamine cell wall structure, and bacterial replication. Proc. Natl. Acad. Sci. USA 97:418-423.
13. Nohno, T., T. Saito, and J. S. Hong. 1986. Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ). Mol. Gen. Genet. 205:260-269.
14. Parish, T., and N. G. Stoker. 1998. Mycobacteria protocols. Humana Press, Totowa, N.J.
15. Pieters, J. 2001. Evasion of host cell defense mechanisms by pathogenic bacteria. Curr. Opin. Immunol. 13:37-44.
16. Russell, D. G. 2001. Mycobacterium tuberculosis: here today, and here tomorrow. Nat. Rev. Mol. Cell Biol. 2:569-577.
17. Steyn, A. J., D. M. Collins, M. K. Hondalus, W. R. Jacobs, Jr., R. P. Kawakami, and B. R. Bloom. 2002. Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host survival but is dispensable for in vivo growth. Proc. Natl. Acad. Sci. USA 99:3147-3152.
18. Tullius, M. V., G. Harth, and M. A. Horwitz. 2003. Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs. Infect. Immun. 71:3927-3936.
19. Walburger, A., A. Koul, G. Ferrari, L. Nguyen, C. Prescianotto-Baschong, K. Huygen, B. Klebl, C. Thompson, G. Bacher, and J. Pieters. 2004. Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 304:1800-1804.