Fibril-mediated adherence of Actinomyces viscosus to saliva-treated hydroxyapatite.
Fibril-mediated adherence of Actinomyces viscosus strain T14V cells to saliva-treated hydroxyapatite was studied. Fibrils were purified by ammonium sulfate precipitation and differential centrifugation from the crude supernatant of whole cells that were sheared by one passage through a French pressure cell. Purified fibrils and crude supernatant inhibited strain T14V adherence to saliva-treated hydroxyapatite to similar extents. However, anti-strain T14V serum and antifibril specific antibody completely abolished strain T14V adherence. The blocking immunoglobulin could be adsorbed from anti-T14V serum by strain T14V whole cells, by purified fibrils, and, to a lesser extent, by cell walls. It was concluded that fibrils mediate adherence of strain T14V cells to saliva-treated hydroxyapatite. In addition, fibril preparations were shown to contain more than 95% protein and to be antigenically homogeneous by immunodiffusion and Laurell rocket immunoelectrophoresis. Purified fibril preparations showed serological identity with the virulence-associated 1 antigen of Lancefield-extracted T14V cells, whereas crude supernatants contained both virulence-associated 1 and virulence-associated 2 antigens, as shown by rocket immunoelectrophoresis.
D000190:Actinomyces / Q000648:ultrastructure*; D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000276:immunology*; D000818:Animals; D000941:Antigens; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006882:Hydroxyapatites / Q000276:immunology*; D007106:Immune Sera; D008854:Microscopy, Electron; D011817:Rabbits; D012463:Saliva / Q000382:microbiology*; D000685:Serum Amyloid A Protein / Q000276:immunology*
D000596:Amino Acids; D000682:Amyloid; D000941:Antigens; D006882:Hydroxyapatites; D007106:Immune Sera; D000685:Serum Amyloid A Protein