This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fenno, J. C.
Right arrow Articles by McBride, B. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fenno, J. C.
Right arrow Articles by McBride, B. C.

 Previous Article  |  Next Article 

Infect Immun, May 1998, p. 1869-1877, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cytopathic Effects of the Major Surface Protein and the Chymotrypsinlike Protease of Treponema denticola

J. Christopher Fenno,1 Pauline M. Hannam,1 W. Keung Leung,2,dagger Muneaki Tamura,1 Veli-Jukka Uitto,2 and Barry C. McBride1,2,*

Department of Microbiology and Immunology1 and Department of Oral Biological and Medical Sciences,2 University of British Columbia, Vancouver, Canada

Received 8 July 1997/Returned for modification 26 September 1997/Accepted 15 January 1998

Prominent antigens of Treponema denticola have been suggested to be mediators of the cytopathic effects typically seen in periodontal disease. In the present study of the T. denticola major surface protein (Msp) and the surface-expressed chymotrypsinlike protease complex (CTLP), we characterized the ability of these proteins to adhere to and lyse epithelial cells. Msp and CTLP were closely associated in spirochete outer membranes. Purified Msp, both native and recombinant, and CTLP bound to glutaraldehyde-fixed periodontal ligament epithelial cells. Adherence of Msp was partially blocked by specific antibodies. Adherence of CTLP was partially blocked by serine protease inhibitors and was further inhibited by specific antibodies. Both native Msp and CTLP were cytotoxic toward periodontal ligament epithelial cells, and their cytotoxicity was inhibited by the same treatments that inhibited adherence. Msp, but not CTLP, lysed erythrocytes. Msp complex (partially purified outer membranes free of protease activity) was cytotoxic toward a variety of different cell types. Pore-forming activities of recombinant Msp in black lipid model membrane assays and in HeLa cell membranes were similar to those reported for the native protein, supporting the hypothesis that Msp cytotoxicity was due to its pore-forming activity.

* Corresponding author. Mailing address: Faculty of Science, University of British Columbia, 6270 University Blvd., Vancouver, B.C. V6T 1Z4, Canada. Phone: (604) 822-3337. Fax: (604) 822-0677. E-mail: mcbride{at}unixg.ubc.ca.

dagger Present address: Department of Periodontology, University of Hong Kong, 3/F Prince Philip Dental Hospital, Hong Kong.

Infect Immun, May 1998, p. 1869-1877, Vol. 66, No. 5
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Nussbaum, G., Ben-Adi, S., Genzler, T., Sela, M., Rosen, G. (2009). Involvement of Toll-Like Receptors 2 and 4 in the Innate Immune Response to Treponema denticola and Its Outer Sheath Components. Infect. Immun. 77: 3939-3947 [Abstract] [Full Text]  
  • McDowell, J. V., Huang, B., Fenno, J. C., Marconi, R. T. (2009). Analysis of a Unique Interaction between the Complement Regulatory Protein Factor H and the Periodontal Pathogen Treponema denticola. Infect. Immun. 77: 1417-1425 [Abstract] [Full Text]  
  • Jun, H.-K., Kang, Y.-M., Lee, H.-R., Lee, S.-H., Choi, B.-K. (2008). Highly Conserved Surface Proteins of Oral Spirochetes as Adhesins and Potent Inducers of Proinflammatory and Osteoclastogenic Factors. Infect. Immun. 76: 2428-2438 [Abstract] [Full Text]  
  • Lai, Y., Chu, L. (2008). Novel Mechanism for Conditional Aerobic Growth of the Anaerobic Bacterium Treponema denticola. Appl. Environ. Microbiol. 74: 73-79 [Abstract] [Full Text]  
  • Bamford, C. V., Fenno, J. C., Jenkinson, H. F., Dymock, D. (2007). The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation. Infect. Immun. 75: 4364-4372 [Abstract] [Full Text]  
  • Jun, H.-K., Lee, H.-R., Lee, S.-H., Choi, B.-K. (2007). Mapping of the proinflammatory domains of MspTL of Treponema lecithinolyticum. Microbiology 153: 2386-2392 [Abstract] [Full Text]  
  • Cameron, C. E., Brouwer, N. L., Tisch, L. M., Kuroiwa, J. M. Y. (2005). Defining the Interaction of the Treponema pallidum Adhesin Tp0751 with Laminin. Infect. Immun. 73: 7485-7494 [Abstract] [Full Text]  
  • Edwards, A. M., Jenkinson, H. F., Woodward, M. J., Dymock, D. (2005). Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405. Infect. Immun. 73: 2891-2898 [Abstract] [Full Text]  
  • Bian, X.-l., Wang, H.-t., Ning, Y., Lee, S. Y., Fenno, J. C. (2005). Mutagenesis of a Novel Gene in the prcA-prtP Protease Locus Affects Expression of Treponema denticola Membrane Complexes. Infect. Immun. 73: 1252-1255 [Abstract] [Full Text]  
  • Lee, S.-H., Kim, K.-K., Choi, B.-K. (2005). Upregulation of Intercellular Adhesion Molecule 1 and Proinflammatory Cytokines by the Major Surface Proteins of Treponema maltophilum and Treponema lecithinolyticum, the Phylogenetic Group IV Oral Spirochetes Associated with Periodontitis and Endodontic Infections. Infect. Immun. 73: 268-276 [Abstract] [Full Text]  
  • Cluss, R. G., Silverman, D. A., Stafford, T. R. (2004). Extracellular Secretion of the Borrelia burgdorferi Oms28 Porin and Bgp, a Glycosaminoglycan Binding Protein. Infect. Immun. 72: 6279-6286 [Abstract] [Full Text]  
  • Ikegami, A., Honma, K., Sharma, A., Kuramitsu, H. K. (2004). Multiple Functions of the Leucine-Rich Repeat Protein LrrA of Treponema denticola. Infect. Immun. 72: 4619-4627 [Abstract] [Full Text]  
  • Amin, M., Ho, A. C. S., Lin, J. Y., Batista da Silva, A. P., Glogauer, M., Ellen, R. P. (2004). Induction of De Novo Subcortical Actin Filament Assembly by Treponema denticola Major Outer Sheath Protein. Infect. Immun. 72: 3650-3654 [Abstract] [Full Text]  
  • Kuramitsu, H. K. (2003). MOLECULAR GENETIC ANALYSIS OF THE VIRULENCE OF ORAL BACTERIAL PATHOGENS: AN HISTORICAL PERSPECTIVE. CROBM 14: 331-344 [Abstract] [Full Text]  
  • Cameron, C. E. (2003). Identification of a Treponema pallidum Laminin-Binding Protein. Infect. Immun. 71: 2525-2533 [Abstract] [Full Text]  
  • Edwards, A. M., Dymock, D., Woodward, M. J., Jenkinson, H. F. (2003). Genetic relatedness and phenotypic characteristics of Treponema associated with human periodontal tissues and ruminant foot disease. Microbiology 149: 1083-1093 [Abstract] [Full Text]  
  • Duncan, M. J. (2003). GENOMICS OF ORAL BACTERIA. CROBM 14: 175-187 [Abstract] [Full Text]  
  • Lee, S. Y., Bian, X.-L., Wong, G. W. K., Hannam, P. M., McBride, B. C., Fenno, J. C. (2002). Cleavage of Treponema denticola PrcA Polypeptide To Yield Protease Complex-Associated Proteins Prca1 and Prca2 Is Dependent on PrtP. J. Bacteriol. 184: 3864-3870 [Abstract] [Full Text]  
  • Fenno, J. C., Lee, S. Y., Bayer, C. H., Ning, Y. (2001). The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola. Infect. Immun. 69: 6193-6200 [Abstract] [Full Text]  
  • Xu, X., Holt, S. C., Kolodrubetz, D. (2001). Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola. Infect. Immun. 69: 4465-4472 [Abstract] [Full Text]  
  • Sela, M. N. (2001). Role of Treponema Denticola in Periodontal Diseases. CROBM 12: 399-413 [Abstract] [Full Text]  
  • Fenno, J. C., Tamura, M., Hannam, P. M., Wong, G. W. K., Chan, R. A., McBride, B. C. (2000). Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment. Infect. Immun. 68: 1884-1892 [Abstract] [Full Text]  
  • Caimano, M. J., Bourell, K. W., Bannister, T. D., Cox, D. L., Radolf, J. D. (1999). The Treponema denticola Major Sheath Protein Is Predominantly Periplasmic and Has Only Limited Surface Exposure. Infect. Immun. 67: 4072-4083 [Abstract] [Full Text]  
  • Wang, Q., Ko, K. S., Kapus, A., McCulloch, C. A. G., Ellen, R. P. (2001). A Spirochete Surface Protein Uncouples Store-operated Calcium Channels in Fibroblasts. A NOVEL CYTOTOXIC MECHANISM. J. Biol. Chem. 276: 23056-23064 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»