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Infection and Immunity, May 2005, p. 2891-2898, Vol. 73, No. 5
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.5.2891-2898.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

Andrew M. Edwards,1,{dagger} Howard F. Jenkinson,1* Martin J. Woodward,2 and David Dymock1

Department of Oral and Dental Science, University of Bristol, Bristol BS1 2LY, United Kingdom,1 Department of Food and Environmental Safety, Veterinary Laboratories Agency, Addlestone KT15 3NB, United Kingdom2

Received 6 August 2004/ Returned for modification 9 November 2004/ Accepted 24 December 2004

There is growing evidence that a number of oral Treponema species, in particular Treponema denticola, are associated with the progression of human periodontal disease. The major sheath (or surface) protein (Msp) of T. denticola is implicated in adhesion of bacteria to host cells and tissue proteins and is likely to be an important virulence factor. However, the binding regions of the Msp are not known. We have purified from Escherichia coli recombinant Msp (rMsp) polypeptides corresponding to the following: full-length Msp (rMsp) minus 13 N-terminal amino acid (aa) residues, an amino-terminal fragment (rN-Msp, 189 aa residues), a 57-aa residue segment from the central region (rV-Msp), and a C-terminal fragment (rC-Msp, 272 aa residues). rMsp (530 aa residues) bound to immobilized fibronectin, keratin, laminin, collagen type I, fibrinogen, hyaluronic acid, and heparin. The N- and V-region polypeptides, but not rC-Msp, also bound to these substrates. Binding of rMsp to fibronectin was targeted to the N-terminal heparin I/fibrin I domain. Antibodies to the N-region or V-region polypeptides, but not antibodies to the rC-Msp fragment, blocked adhesion of T. denticola ATCC 35405 cells to a range of host protein molecules. These results suggest that the N-terminal half of Msp carries epitopes that are surface exposed and that are involved in mediating adhesion. Binding of rMsp onto the cell surface of low-level fibronectin-binding Treponema isolates conferred a 10-fold increase in fibronectin binding. This confirms that Msp functions autonomously as an adhesin and raises the possibility that phenotypic complementation of virulence functions might occur within mixed populations of Treponema species.

* Corresponding author. Mailing address: Oral Microbiology Unit, Department of Oral and Dental Science, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, United Kingdom. Phone: 44 117 9284328. Fax: 44 117 9284313. E-mail: howard.jenkinson{at}bristol.ac.uk.

Editor: V. J. DiRita

{dagger} Present address: Department of Oral Sciences, University of Minnesota, Moos Tower, 515 Delaware St. SE., Minneapolis, MN 55455.

Infection and Immunity, May 2005, p. 2891-2898, Vol. 73, No. 5
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.5.2891-2898.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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