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 Ning, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fenno, J. C.
Right arrow Articles by Ning, Y.

 Previous Article  |  Next Article 

Infection and Immunity, October 2001, p. 6193-6200, Vol. 69, No. 10
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.10.6193-6200.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola

J. Christopher Fenno,1,* Si Young Lee,1,2 Christopher H. Bayer,1 and Yu Ning1

Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48109-1078,1 and Department of Oral Microbiology, College of Dentistry, Kangnung National University, Kangnung, Korea2

Received 9 May 2001/Returned for modification 14 June 2001/Accepted 22 June 2001

High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola, along with Porphyromonas gingivalis and Bacteroides forsythus, are the only cultivatable oral microorganisms that produce significant amounts of "trypsin-like" peptidase activity. The ability of subgingival plaque to hydrolyze N-alpha -benzoyl-DL-arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB, in an apparently noncoding region of the T. denticola genome unannotated contigs (11/2000; http://www.tigr.org). The opdB gene begins with a TTG start codon and encodes a 685-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes. An isogenic T. denticola opdB mutant was constructed by allelic replacement mutagenesis using an ermF/AM gene cassette. The mutant lacked BANA-hydrolyzing activity and had a slightly slower growth rate than the parent strain. This mutant will be used in future studies of interactions of T. denticola with host cells and tissue.

* Corresponding author. Mailing address: Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, MI 48109-1078. Phone: (734) 763-3331. Fax: (734) 764-2425. E-mail: fenno{at}umich.edu.

Infection and Immunity, October 2001, p. 6193-6200, Vol. 69, No. 10
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.10.6193-6200.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • 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]  
  • Yin, L., Dale, B. A. (2007). Activation of protective responses in oral epithelial cells by Fusobacterium nucleatum and human {beta}-defensin-2. J Med Microbiol 56: 976-987 [Abstract] [Full Text]  
  • Miyamoto, M., Ishihara, K., Okuda, K. (2006). The Treponema denticola Surface Protease Dentilisin Degrades Interleukin-1{beta} (IL-1{beta}), IL-6, and Tumor Necrosis Factor Alpha. Infect. Immun. 74: 2462-2467 [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]  
  • Yoshida, A., Nagashima, S., Ansai, T., Tachibana, M., Kato, H., Watari, H., Notomi, T., Takehara, T. (2005). Loop-Mediated Isothermal Amplification Method for Rapid Detection of the Periodontopathic Bacteria Porphyromonas gingivalis, Tannerella forsythia, and Treponema denticola. J. Clin. Microbiol. 43: 2418-2424 [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]  
  • Chung, W. O., Hansen, S. R., Rao, D., Dale, B. A. (2004). Protease-Activated Receptor Signaling Increases Epithelial Antimicrobial Peptide Expression. J. Immunol. 173: 5165-5170 [Abstract] [Full Text]  
  • Correia, F. F., Plummer, A. R., Ellen, R. P., Wyss, C., Boches, S. K., Galvin, J. L., Paster, B. J., Dewhirst, F. E. (2003). Two Paralogous Families of a Two-Gene Subtilisin Operon Are Widely Distributed in Oral Treponemes. J. Bacteriol. 185: 6860-6869 [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]  
  • 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]  
  • Morty, R. E., Fulop, V., Andrews, N. W. (2002). Substrate Recognition Properties of Oligopeptidase B from Salmonella enterica Serovar Typhimurium. J. Bacteriol. 184: 3329-3337 [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»