Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Raynaud, C.
Right arrow Articles by Daffe, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Raynaud, C.
Right arrow Articles by Daffe, M.
Agricola
Right arrow Articles by Raynaud, C.
Right arrow Articles by Daffe, M.

microbiology, Vol 144, 577-587, Copyright © 1998 by Society for General Microbiology

ARTICLES

Extracellular enzyme activities potentially involved in the pathogenicity of Mycobacterium tuberculosis

C Raynaud, G Etienne, P Peyron, MA Laneelle and M Daffe
Institut de Pharmacologie et de Biologie Structurale, CNRS, Toulouse, France.

To evaluate the potential contribution of extracellular enzymes to the pathogenicity of mycobacteria, the presence of selected enzyme activities was investigated in the culture filtrates of the obligate human pathogen Mycobacterium tuberculosis, M. bovis BCG, the opportunistic pathogens M. kansasii and M. fortuitum, and the non- pathogenic species M. phlei and M. smegmatis. For M. tuberculosis and M. bovis, 22 enzyme activities were detected in the culture filtrates and/or cell surfaces, of which eight were absent from the culture fluids of non-pathogens: alanine dehydrogenase, glutamine synthetase, nicotinamidase, isonicotinamidase, superoxide dismutase, catalase, peroxidase and alcohol dehydrogenase. These activities, which correspond to secreted enzymes, formed a significant part (up to 92%) of the total enzyme activities of the bacteria and were absent from the culture fluids and the cell surfaces of the non-pathogenic species M. smegmatis and M. phlei. The extracellular location of superoxide dismutase and glutamine synthetase seemed to be restricted to the obligate pathogens examined. The difference in the enzyme profiles was not attributable to the growth rates of the two groups of bacteria. The presence of the eight enzyme activities in the outermost compartments of obligate pathogens and their absence in those of non-pathogens provides further evidence that these enzymes may be involved in the pathogenicity of mycobacteria. In addition, the eight enzyme activities were demonstrated in the cell extract of M. smegmatis. Stepwise erosion of the cell surface of M. smegmatis to expose internal capsular constituents showed that the various enzyme activities, with the possible exception of superoxide dismutase, were located more deeply in the cell envelope of this bacterium. This suggests that the molecular architecture of the mycobacterial envelopes may play an important role in the pathogenicity of these organisms.


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
B. Schiffler, E. Barth, M. Daffe, and R. Benz
Corynebacterium diphtheriae: Identification and Characterization of a Channel-Forming Protein in the Cell Wall
J. Bacteriol., November 1, 2007; 189(21): 7709 - 7719.
[Abstract] [Full Text] [PDF]

Home page
 J Biomol ScreenHome page
U. Singh and D. Sarkar
Development of a Simple High-Throughput Screening Protocol Based on Biosynthetic Activity of Mycobacterium tuberculosis Glutamine Synthetase for the Identification of Novel Inhibitors
J Biomol Screen, December 1, 2006; 11(8): 1035 - 1042.
[Abstract] [PDF]

Home page
 Infect. Immun.Home page
R. A. Brady, J. G. Leid, A. K. Camper, J. W. Costerton, and M. E. Shirtliff
Identification of Staphylococcus aureus Proteins Recognized by the Antibody-Mediated Immune Response to a Biofilm Infection.
Infect. Immun., June 1, 2006; 74(6): 3415 - 3426.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
J. A. McDonough, K. E. Hacker, A. R. Flores, M. S. Pavelka Jr, and M. Braunstein
The Twin-Arginine Translocation Pathway of Mycobacterium smegmatis Is Functional and Required for the Export of Mycobacterial {beta}-Lactamases
J. Bacteriol., November 15, 2005; 187(22): 7667 - 7679.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
B. R. Sellman, A. P. Howell, C. Kelly-Boyd, and S. M. Baker
Identification of Immunogenic and Serum Binding Proteins of Staphylococcus epidermidis
Infect. Immun., October 1, 2005; 73(10): 6591 - 6600.
[Abstract] [Full Text] [PDF]

Home page
 J Biomol ScreenHome page
U. Singh, V. Panchanadikar, and D. Sarkar
Development of a Simple Assay Protocol for High-Throughput Screening of Mycobacterium tuberculosis Glutamine Synthetase for the Identification of Novel Inhibitors
J Biomol Screen, October 1, 2005; 10(7): 725 - 729.
[Abstract] [PDF]

Home page
 MicrobiologyHome page
G. Etienne, F. Laval, C. Villeneuve, P. Dinadayala, A. Abouwarda, D. Zerbib, A. Galamba, and M. Daffe
The cell envelope structure and properties of Mycobacterium smegmatis mc2155: is there a clue for the unique transformability of the strain?
Microbiology, June 1, 2005; 151(6): 2075 - 2086.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
I. Vergne, J. Chua, H.-H. Lee, M. Lucas, J. Belisle, and V. Deretic
Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis
PNAS, March 15, 2005; 102(11): 4033 - 4038.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Mehta, J. T. Pearson, S. Mahajan, A. Nath, M. J. Hickey, D. R. Sherman, and W. M. Atkins
Adenylylation and Catalytic Properties of Mycobacterium tuberculosis Glutamine Synthetase Expressed in Escherichia coli versus Mycobacteria
J. Biol. Chem., May 21, 2004; 279(21): 22477 - 22482.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Villeneuve, G. Etienne, V. Abadie, H. Montrozier, C. Bordier, F. Laval, M. Daffe, I. Maridonneau-Parini, and C. Astarie-Dequeker
Surface-exposed Glycopeptidolipids of Mycobacterium smegmatis Specifically Inhibit the Phagocytosis of Mycobacteria by Human Macrophages: IDENTIFICATION OF A NOVEL FAMILY OF GLYCOPEPTIDOLIPIDS
J. Biol. Chem., December 19, 2003; 278(51): 51291 - 51300.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
R. C. Huard, S. Chitale, M. Leung, L. C. O. Lazzarini, H. Zhu, E. Shashkina, S. Laal, M. B. Conde, A. L. Kritski, J. T. Belisle, et al.
The Mycobacterium tuberculosis Complex-Restricted Gene cfp32 Encodes an Expressed Protein That Is Detectable in Tuberculosis Patients and Is Positively Correlated with Pulmonary Interleukin-10
Infect. Immun., December 1, 2003; 71(12): 6871 - 6883.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
G. Etienne, C. Villeneuve, H. Billman-Jacobe, C. Astarie-Dequeker, M.-A. Dupont, and M. Daffe
The impact of the absence of glycopeptidolipids on the ultrastructure, cell surface and cell wall properties, and phagocytosis of Mycobacterium smegmatis
Microbiology, October 1, 2002; 148(10): 3089 - 3100.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
Z. Feng, N. E. Caceres, G. Sarath, and R. G. Barletta
Mycobacterium smegmatisL-Alanine Dehydrogenase (Ald) Is Required for Proficient Utilization of Alanine as a Sole Nitrogen Source and Sustained Anaerobic Growth
J. Bacteriol., September 15, 2002; 184(18): 5001 - 5010.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
C. H. Johnson, M. G. Klotz, J. L. York, V. Kruft, and J. E. McEwen
Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases
Microbiology, April 1, 2002; 148(4): 1129 - 1142.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
K. Chan, T. Knaak, L. Satkamp, O. Humbert, S. Falkow, and L. Ramakrishnan
Complex pattern of Mycobacterium marinum gene expression during long-term granulomatous infection
PNAS, March 19, 2002; 99(6): 3920 - 3925.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
C. Recchi, J. Rauzier, B. Gicquel, and J.-M. Reyrat
Signal-sequence-independent secretion of the staphylococcal nuclease in Mycobacterium smegmatis
Microbiology, February 1, 2002; 148(2): 529 - 536.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
M. V. Tullius, G. Harth, and M. A. Horwitz
High Extracellular Levels of Mycobacterium tuberculosis Glutamine Synthetase and Superoxide Dismutase in Actively Growing Cultures Are Due to High Expression and Extracellular Stability Rather than to a Protein-Specific Export Mechanism
Infect. Immun., October 1, 2001; 69(10): 6348 - 6363.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. L. Dahl, J. Wei, J. W. Moulder, S. Laal, and R. L. Friedman
Subcellular Localization of the Intracellular Survival-Enhancing Eis Protein of Mycobacterium tuberculosis
Infect. Immun., July 1, 2001; 69(7): 4295 - 4302.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
V. Puech, M. Chami, A. Lemassu, M.-A. Lanéelle, B. Schiffler, P. Gounon, N. Bayan, R. Benz, and M. Daffé
Structure of the cell envelope of corynebacteria: importance of the non-covalently bound lipids in the formation of the cell wall permeability barrier and fracture plane
Microbiology, May 1, 2001; 147(5): 1365 - 1382.
[Abstract] [Full Text]

Home page
 J. Bacteriol.Home page
M. T. Saleh and J. T. Belisle
Secretion of an Acid Phosphatase (SapM) by Mycobacterium tuberculosis That Is Similar to Eukaryotic Acid Phosphatases
J. Bacteriol., December 1, 2000; 182(23): 6850 - 6853.
[Abstract] [Full Text]

Home page
 J. Bacteriol.Home page
H. I. M. Boshoff and V. Mizrahi
Expression of Mycobacterium smegmatis Pyrazinamidase in Mycobacterium tuberculosis Confers Hypersensitivity to Pyrazinamide and Related Amides
J. Bacteriol., October 1, 2000; 182(19): 5479 - 5485.
[Abstract] [Full Text]

Home page
 J. Bacteriol.Home page
M. Braunstein, T. J. Griffin IV, J. I. Kriakov, S. T. Friedman, N. D. F. Grindley, and W. R. Jacobs Jr.
Identification of Genes Encoding Exported Mycobacterium tuberculosis Proteins Using a Tn552'phoA In Vitro Transposition System
J. Bacteriol., May 15, 2000; 182(10): 2732 - 2740.
[Abstract] [Full Text]

Home page
 J. Bacteriol.Home page
H. I. M. Boshoff and V. Mizrahi
Purification, Gene Cloning, Targeted Knockout, Overexpression, and Biochemical Characterization of the Major Pyrazinamidase from Mycobacterium smegmatis
J. Bacteriol., November 15, 1998; 180(22): 5809 - 5814.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
L. R. Camacho, P. Constant, C. Raynaud, M.-A. Laneelle, J. A. Triccas, B. Gicquel, M. Daffe, and C. Guilhot
Analysis of the Phthiocerol Dimycocerosate Locus of Mycobacterium tuberculosis. EVIDENCE THAT THIS LIPID IS INVOLVED IN THE CELL WALL PERMEABILITY BARRIER
J. Biol. Chem., June 1, 2001; 276(23): 19845 - 19854.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1998 Society for General Microbiology.