Volume 151, Issue 1 pp. 59-64

Identification of an elastolytic protease in stationary phase culture filtrates of M. tuberculosis

Sharon S Rowland,

Corresponding Author

Sharon S Rowland

Department of Medical and Research Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA

Corresponding author. Fax: (1) (410) 706-5229; e-mail: [email protected]Search for more papers by this author

Jennifer L Ruckert,

Jennifer L Ruckert

Department of Medical and Research Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA

Search for more papers by this author

Bryan N Burall Jr.,

Bryan N Burall Jr.

Department of Microbiology, University of Maryland Dental School, Baltimore, MD 21201, USA

Search for more papers by this author

Sharon S Rowland,

Corresponding Author

Sharon S Rowland

Department of Medical and Research Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA

Corresponding author. Fax: (1) (410) 706-5229; e-mail: [email protected]Search for more papers by this author

Jennifer L Ruckert,

Jennifer L Ruckert

Department of Medical and Research Technology, University of Maryland School of Medicine, Baltimore, MD 21201, USA

Search for more papers by this author

Bryan N Burall Jr.,

Bryan N Burall Jr.

Department of Microbiology, University of Maryland Dental School, Baltimore, MD 21201, USA

Search for more papers by this author

First published: 17 January 2006

https://doi.org/10.1111/j.1574-6968.1997.tb10394.x

Share a link

Email
Wechat
Bluesky

Abstract

Culture filtrate from M. tuberculosis grown in Sauton broth was screened at weekly intervals for elastase and caseinase activity. Both activities were detected concomitantly at 4 weeks and had similar inhibitor and pH profiles. Highest activity occurred between pH 6.5 and pH 7.5. Azocaseinase activity was linear with time between 12 and 28 h at 37°C. Enzymatic activity was inhibited by EDTA, EGTA, dithiothreitol, ethylmaleimide, 1,10-phenanthroline, Zincov™, N-tosyl-l-phenylalanine chloromethyl ketone, and N-methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone. SDS-PAGE analysis revealed breakdown of casein after incubation with culture filtrate. These results indicate the presence of a calcium-dependent, elastolytic metalloprotease in stationary phase cultures of M. tuberculosis.

References

1 Dannenberg Jr., A.M. and Rook, G.A.W. (1994) Pathogenesis of pulmonary tuberculosis. In: Tuberculosis (Bloom, B.R., Ed.), pp. 459–483. ASM Press, Washington, DC.
Google Scholar
2 Goguen, J.D., Hoe, N.P., and Subrahmanyam, Y.V. (1995) Proteases and bacterial virulence: a view from the trenches. Infect. Agents Dis. 4, 47–54.
PubMed Web of Science® Google Scholar
3 Travis, J., Potempa, J., and Maeda, H. (1995) Are bacterial proteinases pathogenic factors? Trends Microbiol. 3, 405–407.
Google Scholar
4 Lomholt, H. and Kilian, M. (1993) Antigenic relationships among immunoglobulin A1 proteases from Haemophilus, Neisseria, and Streptococcus species. Infect. Immun. 62, 3178–3183.
PubMed Web of Science® Google Scholar
5 Sojar, H.T., Lee, J-Y, Bedi, G.D., and Genco, R.J. (1993) Purification and characterization of a protease from Porphyromonas gingivalis capable of degrading salt-solubilized collagen. Infect. Immun. 61, 2369–2376.
CAS PubMed Web of Science® Google Scholar
6 Wretland, B., and Pavlovskis, O.R. (1983) Pseudomonas aeruginosa elastase and its role in Pseudomonas infections. Rev. Infect. Dis. 5 (Suppl.), 998–1004.
Google Scholar
7 Henderson, B. and Hall, N.D. (1991) Metalloproteinases: Role in pathology and development of inhibitors. Agents and Actions 34, 324–328.
10.1007/BF01988723
CAS PubMed Web of Science® Google Scholar
8 Monod, M., Paris, S., Sanglard, D., Jaton-Ogay, K., Bille, J., and Latge, J.P. (1993) Isolation and characterization of a secreted metalloprotease of Aspergillus fumigatus. Infect. Immunol. 61, 4099–4104.
CAS PubMed Web of Science® Google Scholar
9 Olson, J.C. and Ohman, D.E. (1992) Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ions. J. Bacteriol. 174, 4140–4147.
10.1128/jb.174.12.4140-4147.1992
CAS PubMed Web of Science® Google Scholar
10 Kannan, K.B., Katoch, V.M., Sharma, V.D., and Bharadwaj, V.P. (1987) Extracellular enzymes of mycobacteria. FEMS Miobiol. Lett. 48, 31–33.
10.1111/j.1574-6968.1987.tb02510.x
CAS Web of Science® Google Scholar
11 Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.
10.1111/j.1462-5822.2007.00901.x
CAS PubMed Web of Science® Google Scholar
12 Wayne, L.G. 1994. Cultivation of Mycobacterium tuberculosis for research purposes. In: Tuberculosis (Bloom, B.R., Ed.), pp. 73–83, ASM Press, Washington, DC.
Google Scholar
13 Hase, C.C. and Finkelstein, R.A. (1993) Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57, 823–837.
10.1128/MMBR.57.4.823-837.1993
CAS PubMed Web of Science® Google Scholar
14 Karunakaran, T. and Devi, B.G. (1995) Proteolytic activity of Aeromonas caviae, J. Basic Microbiol. 35, 241–247.
10.1002/jobm.3620350409
CAS PubMed Web of Science® Google Scholar
15 Gobin, J., Moore, C.H., Reeve, Jr., J.R., Wong, D.K., Gibson, B.W., and Horwitz, M.A. (1995) Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc. Natl. Acad. Sci. USA 92, 5189–5193.
10.1073/pnas.92.11.5189
CAS PubMed Web of Science® Google Scholar
16 Young, D., T. Garbe, R. Lathigra, and C. Abou-Zeid. 1990. Protein antigens: structure, function and regulation. In: Molecular Biology of the Mycobacteria (J. McFadden, Ed.), pp. 1–35. Academic Press, London.
Google Scholar
17 Neurath, H. (1993) The diversity of proteolytic enzymes. In: Proteolytic Enzymes, A Practical Approach (Beynon, R.J. and Bond, J.S., Eds.), pp. 1–13. Oxford University Press, Oxford.
Google Scholar
18 Kothary, M.H. (1985) Production and partial characterization of an elastolytic protease of Vibrio vulnificus. Infect. Immunol. 50, 534–540.
CAS PubMed Web of Science® Google Scholar
19 Rust, L., Messing, C.R., and Iglewski, B.H. (1994). Elastase activities. In: Bacterial Pathogenesis — Methods in Enzymology (Clark, V.L. and Bavoil, P.M., Eds.), Vol. 235, pp. 554–562, Academic Press, San Diego.
Google Scholar
20 Sidler, W., Kumpf, B., Peterhans, B. and Zuber, H. (1986) A neutral proteinase produced by Bacillus cereus with high sequence homology to thermolysin. Appl. Microbiol. Biotechnol. 25, 18–24.
10.1007/BF00252506
CAS Web of Science® Google Scholar

Volume151, Issue1

June 1997

Pages 59-64

Identification of an elastolytic protease in stationary phase culture filtrates of M. tuberculosis

Abstract

References

References

Information

About Wiley Online Library

Help & Support

Opportunities

Connect with Wiley

Identification of an elastolytic protease in stationary phase culture filtrates of M. tuberculosis

Abstract

References

References

Related

Information