title: Activation of complement by Treponema denticola.
abstract: Oral spirochetes have been shown to be associated with periodontal diseases and are present in increased numbers in lesions of greater severity. In this study, the interaction of Treponema denticola with human complement, a major antibacterial defense system, was examined. For each of two strains of T. denticola, it was found that both the classical and alternative pathways of human complement were activated in human serum upon incubation at 37 degrees C. C3 fragments were deposited on the surface of this organism following complement activation; the fragments bound included both of the major C3-derived opsonic fragments C3b and iC3b. Under incubation conditions identical to those carried out for complement activation in serum, T. denticola failed to degrade purified, hemolytically-active C3, although it readily degraded inactivated C3. Thus, despite the documented proteolytic activity of this organism, complement activation and deposition of complement-derived opsonins may be important defense mechanisms in the control of infections with T. denticola.
authors.affiliation: Virginia Commonwealth University, School of Dentistry, Richmond 23298.
authors.forename: H A
authors.initials: HA
authors.lastname: Schenkein
authors.forename: C R
authors.initials: CR
authors.lastname: Berry
mesh_terms: D003176:Complement C3 / Q000276:immunology; D003179:Complement C3b / Q000302:isolation & purification; D003181:Complement C4 / Q000276:immunology; D015941:Complement Hemolytic Activity Assay; D003170:Complement Pathway, Alternative / Q000276:immunology*; D003171:Complement Pathway, Classical / Q000276:immunology*; D003773:Dental Plaque / Q000382:microbiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009895:Opsonin Proteins / Q000302:isolation & purification; D014208:Treponema / Q000276:immunology* / Q000472:pathogenicity
chemical_list: D003176:Complement C3; D003181:Complement C4; D009895:Opsonin Proteins; D003179:Complement C3b