Glutamine synthetase encoded by glnA-1 is necessary for cell wall resistance and pathogenicity of Mycobacterium bovis

Microbiology

Volumn 156, Issue 12, 2010, Pages 3669-3677

  Chandra, Harish ^a   Basir, Seemi Farhat ^b   Gupta, Manish ^a   Banerjee, Nirupama ^a  

^a INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^b JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLOSERINE; ETHAMBUTOL; GLNA 1 PROTEIN; GLUTAMATE AMMONIA LIGASE; GLUTAMINE; ISONIAZID; LYSOZYME; POLYACRYLAMIDE; POLYGLUTAMINE; POLYSTYRENE; RIFAMPICIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL CELL WALL; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BIOFILM; CHEMICAL STRESS; CONTROLLED STUDY; DISEASE DURATION; HUMAN; HUMAN CELL; MACROPHAGE; MALE; MINIMUM INHIBITORY CONCENTRATION; MOUSE; MUTANT; MYCOBACTERIUM BOVIS; MYCOBACTERIUM SMEGMATIS; NONHUMAN; PHYSICAL STRESS; PRIORITY JOURNAL; SUPPLEMENTATION; ULTRASOUND; WILD TYPE;

ANIMALS; BACTERIAL PROTEINS; CELL LINE; CELL WALL; GLUTAMATE-AMMONIA LIGASE; HUMANS; MACROPHAGES; MALE; MICE; MICE, INBRED BALB C; MYCOBACTERIUM BOVIS; PEPTIDES; TUBERCULOSIS;

CORYNEBACTERINEAE; MUS; MYCOBACTERIUM BOVIS; MYCOBACTERIUM SMEGMATIS;

EID: 78650072476     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.043828-0     Document Type: Article

References (31)

1. Amon, J., Titgemeyer, F. & Burkovski, A. (2009). A genomic view on nitrogen metabolism and nitrogen control in mycobacteria. J Mol Microbiol Biotechnol 17, 20-29.
2. Candela, T. & Fouet, A. (2006). Poly-gamma-glutamate in bacteria. Mol Microbiol 60, 1091-1098.
3. 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 genome sequence. Nature 393, 537-544.
4. Fisher, S. H. (1999). Regulation of nitrogen metabolism in Bacillus subtilis: vive la difference! Mol Microbiol 32, 223-232.
5. Flynn, J. L. & Chan, J. (2001). Tuberculosis: latency and reactivation. Infect Immun 69, 4195-4201.
6. Garnier, T., Eiglmeier, K., Camus, J. C., Medina, N., Mansoor, H., Pryor, M., Duthoy, S., Grondin, S., Lacroix, C. & other authors (2003). The complete genome sequence of Mycobacterium bovis. Proc Natl Acad Sci U S A 100, 7877-7882.
7. Hanson, C. W. & Martin, W. J. (1978). Modified agar dilution method for rapid antibiotic susceptibility testing of anaerobic bacteria. Antimicrob Agents Chemother 13, 383-388.
8. Harper, C., Hayward, D., Wild, I. & Helden, P. V. (2008). Regulation of nitrogen metabolism in Mycobacterium tuberculosis: a comparision with mechanisms in Corynebacterium glutamicum and Streptomyces coelicolor. IUBMB Life 60, 643-650.
9. Harth, G. & Horwitz, M. A. (1999). An inhibitor of exported Mycobacterium tuberculosis glutamine synthetase selectively blocks the growth of pathogenic Mycobacterium in axenic culture and in human monocytes: extracellular proteins as potential novel drug targets. J Exp Med 189, 1425-1436.
10. Harth, G., Clemens, D. L. & Horwitz, M. A. (1994). Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity. Proc Natl Acad Sci U S A 91, 9342-9346.
11. Harth, G., Zamecnik, P. C., Tang, J. Y., Tabatadze, D. & Horwitz, M. A. (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 U S A 97, 418-423. (Pubitemid 30055846)
12. Harth, G., Masleša-Galić, S., Tullius, M. V. & Horwitz, M. A. (2005). All four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis. Mol Microbiol 58, 1157-1172.
13. Hett, E. C. & Rubin, E. J. (2008). Bacterial growth and cell division: a mycobacterial perspective. Microbiol Mol Biol Rev 72, 126-156.
14. Hirschfield, G. R., McNeil, M. & Brennan, P. J. (1990). Peptidoglyc-anassociated polypeptides of Mycobacterium tuberculosis. J Bacteriol 172, 1005-1013.
15. Howard, N. S., Gomez, J. E., Ko, C. & Bishai, W. R. (1995). Color selection with a hygromycin-resistance-based Escherchia coli-mycobacterial shuttle vector. Gene 166, 181-182.
16. Krajewski, W. W., Collins, R., Holmberg-Schiavone, L., Jones, A., Karlberg, T. & Mowbray, S. L. (2008). Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design. J Mol Biol 375, 217-228.
17. MacKenzie, S. L. & Hogge, L. R. (1977). Gas chromatography mass spectrometry of the N(O)-heptafluorobutyryl isobutyl esters of the protein amino acids using electron impact ionization. J Chromatogr 132, 485-493.
18. Merrick, M. J. & Edwards, R. A. (1995). Nitrogen control in bacteria. Microbiol Rev 59, 604-622.
19. Ojha, A., Anand, M., Bhatt, A., Kremer, L., Jacobs, W. R., Jr & Hatfull, G. F. (2005). GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria. Cell 123, 861-873.
20. Ojha, A. K., Baughn, A. D., Sambandan, D., Hsu, T., Trivelli, X., Guerardel, Y., Alahari, A., Kremer, L., Jacobs, W. R., Jr & Hatfull, G. F. (2008). Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug-tolerant bacteria. Mol Microbiol 69, 164-174. (Pubitemid 351832764)
21. O'Toole, G. A., Pratt, L. A., Watnick, P. I., Newman, D. K., Weaver, V. B. & Kolter, R. (1999). Genetic approaches to study of biofilms. Methods Enzymol 310, 91-109.
22. Palomino, J. C., Martin, A., Camacho, M., Guerra, H., Swings, J. & Portaels, F. (2002). Resazurin microtiter assay plate: simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis. Antimicrob Agents Chemother 46, 2720-2722. (Pubitemid 34793497)
23. Pavelka, M. S., Jr & Jacobs, W. R., Jr (1999). Comparison of the construction of unmarked deletion mutations in Mycobacterium smegmatis, Mycobacterium bovis Bacillus Calmette-Guérin, and Mycobacterium tuberculosis H37Rv by allelic exchange. J Bacteriol 181, 4780-4789.
24. Pelicic, V., Jackson, M., Reyrat, J. M., Jacobs, W. R., Jr, Gicquel, B. & Guilhot, C. (1997). Efficient allelic exchange and transposon mutagenesis in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 94, 10955-10960.
25. Reitzer, L. J. (1996). Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, L-alanine, and D-alanine. In Escherichia coli and Salmonella typhimurium, 2nd edn, pp. 391-407. Edited by F. C. Neidhardt & R. Curtiss. Washington, DC: American Society for Microbiology.
26. Theus, S. A., Cave, M. D. & Eisenach, K. D. (2004). Activated THP-1 cells: an attractive model for the assessment of intracellular growth rates of Mycobacterium tuberculosis isolates. Infect Immun 72, 1169-1173.
27. Tullius, M. V., Harth, G. & Horwitz, M. A. (2003). Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs. Infect Immun 71, 3927-3936.
28. Vandal, O. H., Roberts, J. A., Odaira, T., Schnappinger, D., Nathan, C. F. & Ehrt, S. (2009). Acid-susceptible mutants of Mycobacterium tuberculosis share hypersusceptibility to cell wall and oxidative stress and to the host environment. J Bacteriol 191, 625-631.
29. Wietzerbin, J., Lederer, F. & Petit, J. F. (1975). Structural study of the poly-L-glutamic acid of the cell wall of Mycobacterium tuberculosis var hominis, strain Brevannes. Biochem Biophys Res Commun 62, 246-252.
30. Woolfolk, C. A., Shapiro, B. & Stadtman, E. R. (1966). Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli. Arch Biochem Biophys 116, 177-192.
31. Yamazaki, Y., Danelishvili, L., Wu, M., MacNab, M. & Bermudez, L. E. (2006). Mycobacterium avium genes associated with the ability to form a biofilm. Appl Environ Microbiol 72, 819-825.