|
|
||||||||

1 Oral Microbiology Unit, Department of Oral and Dental Science, University of Bristol Dental School, Lower Maudlin Street, Bristol BS1 2LY, UK
2 Molecular Genetics Unit, Department of Bacterial Diseases, Veterinary Laboratories Agency (Weybridge), Woodham Lane, Addlestone, Surrey KT15 3NB, UK
Correspondence
Howard F. Jenkinson
howard.jenkinson{at}bris.ac.uk
Treponema have been implicated recently in the pathogenesis of digital dermatitis (DD) and contagious ovine digital dermatitis (CODD) that are infectious diseases of bovine and ovine foot tissues, respectively. Previous analyses of treponemal 16S rDNA sequences, PCR-amplified directly from DD or CODD lesions, have suggested relatedness of animal Treponema to some human oral Treponema species isolated from periodontal tissues. In this study a range of adhesion and virulence-related properties of three animal Treponema isolates have been compared with representative human oral strains of Treponema denticola and Treponema vincentii. In adhesion assays using biotinylated treponemal cells, T. denticola cells bound in consistently higher numbers to fibronectin, laminin, collagen type I, gelatin, keratin and lactoferrin than did T. vincentii or animal Treponema isolates. However, animal DD strains adhered to fibrinogen at equivalent or greater levels than T. denticola. All Treponema strains bound to the amino-terminal heparin I/fibrin I domain of fibronectin. 16S rDNA sequence analyses placed ovine strain UB1090 and bovine strain UB1467 within a cluster that was phylogenetically related to T. vincentii, while ovine strain UB1466 appeared more closely related to T. denticola. These observations correlated with phenotypic properties. Thus, T. denticola ATCC 35405, GM-1, and Treponema UB1466 had similar outer-membrane protein profiles, produced chymotrypsin-like protease (CTLP), trypsin-like protease and high levels of proline iminopeptidase, and co-aggregated with human oral bacteria Porphyromonas gingivalis and Streptococcus crista. Conversely, T. vincentii ATCC 35580, D2A-2, and animal strains UB1090 and UB1467 did not express CTLP or trypsin-like protease and did not co-aggregate with P. gingivalis or S. crista. Taken collectively, these results suggest that human oral-related Treponema have broad host specificity and that similar control or preventive strategies might be developed for human and animal Treponema-associated infections.
The GenBank accession numbers for the 16S rDNA sequences reported in this paper are AY119692 (Treponema denticola GM-1), AY119690 (Treponema vincentii D2A-2), AF363634 (Treponema sp. UB1466, previously designated G179) and AY119691 (Treponema sp. UB1467).
Present address: Department of Pathology and Microbiology, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK.
This article has been cited by other articles:
![]() |
M. K. Elliott, D. P. Alt, and R. L. Zuerner Lesion Formation and Antibody Response Induced by Papillomatous Digital Dermatitis-Associated Spirochetes in a Murine Abscess Model Infect. Immun., September 1, 2007; 75(9): 4400 - 4408. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. V. Bamford, J. C. Fenno, H. F. Jenkinson, and D. Dymock The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation Infect. Immun., September 1, 2007; 75(9): 4364 - 4372. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. M. Edwards, H. F. Jenkinson, M. J. Woodward, and D. Dymock Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405 Infect. Immun., May 1, 2005; 73(5): 2891 - 2898. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |