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Infection and Immunity, April 2000, p. 1884-1892, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

J. Christopher Fenno,1,* Muneaki Tamura,1 Pauline M. Hannam,1 Grace W. K. Wong,1 Roger A. Chan,1 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 29 September 1999/Returned for modification 24 November 1999/Accepted 13 December 1999

Proteins secreted or exported by Treponema denticola have been implicated as mediators of specific interactions between the spirochete and subgingival tissues in periodontal diseases. However, limited information is available on the ability of this peptidolytic organism to bind or transport soluble peptides present in the subgingival environment. A prominent 70-kDa protein was isolated from surface extracts of T. denticola ATCC 35405. A clone expressing a portion of the protein was identified in an Escherichia coli expression library of T. denticola DNA. DNA sequence analysis showed that the cloned gene encoded a peptide homologous to OppA, the solute binding protein of an ATP-binding cassette-type peptide transporter involved in peptide uptake and environmental signaling in a wide range of bacteria. Genes encoding OppB, -C, -D, and -F were identified directly downstream of oppA in T. denticola. OppA was present in representative strains of T. denticola and in Treponema vincentii but was not detected in Treponema pectinovorum or Treponema socranskii. Immunogold electron microscopy suggested that OppA was accessible to proteins at the surface of the spirochete. Native OppA bound soluble plasminogen and fibronectin but did not bind to immobilized substrates or epithelial cells. A T. denticola oppA mutant bound reduced amounts of soluble plasminogen, and plasminogen binding to the parent strain was inhibited by the lysine analog varepsilon -aminocaproic acid. Binding of soluble host proteins by OppA may be important both for spirochete-host interactions in the subgingival environment and for uptake of peptide nutrients.

* Corresponding author. Present address: Department of Biologic and Materials Sciences, School of Dentistry, 1011 N. University Ave., University of Michigan, Ann Arbor, MI 48109. Phone: (734) 763-3331. Fax: (734) 764-2425. E-mail: fenno{at}umich.edu.

Infection and Immunity, April 2000, p. 1884-1892, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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