Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola.
Interactions with fibronectin are important in the virulence strategies of a range of disease-related bacteria. The periodontitis-associated oral spirochaete Treponema denticola expresses at least two fibronectin-binding proteins, designated Msp (major surface protein) and OppA (oligopeptide-binding protein homologue). To identify other T. denticola outer membrane fibronectin-binding proteins, the amino acid sequence of the Treponema pallidum fibronectin-binding protein Tp0155 was used to survey the T. denticola genome. Seven T. denticola genes encoding orthologous proteins were identified. All but two were expressed in Escherichia coli and purified recombinant proteins bound fibronectin. Using antibodies to the N-terminal region of Tp0155, it was demonstrated that T. denticola TDE2318, with highest homology to Tp0155, was cell surface localized. Like Tp0155, the seven T. denticola proteins contained an M23 peptidase domain and four (TDE2318, TDE2753, TDE1738, TDE1297) contained one or two LysM domains. M23 peptidases can degrade peptidoglycan whereas LysM domains recognize carbohydrate polymers. In addition, TDE1738 may act as a bacteriocin based on homology with other bacterial lysins and the presence of an adjacent gene encoding a putative immunity factor. Collectively, these results suggest that T. denticola expresses fibronectin-binding proteins associated with the cell surface that may also have cell wall modifying or lytic functions.
Oral Microbiology Unit, Department of Oral and Dental Science, University of Bristol, Bristol, UK. caroline.bamford@bristol.ac.uk
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Bamford
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Francescutti
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Cameron
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Jenkinson
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Dymock
D018829:Adhesins, Bacterial / Q000032:analysis*; D020816:Amino Acid Motifs / Q000235:genetics; D001422:Bacterial Adhesion / Q000235:genetics; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis; D001430:Bacteriocins / Q000378:metabolism; D015153:Blotting, Western; D002352:Carrier Proteins / Q000032:analysis; D016384:Consensus Sequence / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D005353:Fibronectins / Q000032:analysis*; D016680:Genome, Bacterial / Q000235:genetics; D006801:Humans; D008074:Lipoproteins / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D009842:Oligopeptides / Q000032:analysis; D016366:Open Reading Frames / Q000235:genetics; D010447:Peptide Hydrolases / Q000032:analysis*; D010457:Peptidoglycan / Q000378:metabolism; D010957:Plasmids / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D048373:Treponema denticola / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D014210:Treponema pallidum / Q000235:genetics
D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D001430:Bacteriocins; D002352:Carrier Proteins; D005353:Fibronectins; D008074:Lipoproteins; D008565:Membrane Proteins; D009842:Oligopeptides; D010457:Peptidoglycan; C078635:fibronectin-binding proteins, bacterial; C046506:oligopeptide-binding protein, bacteria; D010447:Peptide Hydrolases