title: Fimbriae of Porphyromonas gingivalis induce opsonic antibodies that significantly enhance phagocytosis and killing by human polymorphonuclear leukocytes.
abstract: Porphyromonas gingivalis has been strongly implicated in the pathogenesis of human periodontitis. Fimbriae mediate adherence and colonization of the oral cavity by this organism and may, therefore, have potential for use as antigen in an anti-P. gingivalis vaccine. The purpose of our study was to determine whether P. gingivalis fimbriae have opsonic target sites and whether they are accessible on the cell surfaces and cross-reactive among P. gingivalis fimbrial types and serotypes. Rabbits were immunized with a vaccine. The antiserum reacted with a 43-kDa fimbrillin monomer and a 43-kDa component in whole-cell sonicates of P. gingivalis 33277, but it showed only very weak reactivity in the 43-kDa region of Western blots of a whole-cell sonicate of strain DPG3, a mutant that does not express functional fimbriae. The antibody enhanced chemiluminescence approximately six-fold relative to preimmune serum values and significantly enhanced phagocytosis and killing of P. gingivalis 33277 by human polymorphonuclear leukocytes. Peak opsonic activity was observed at week 6 followed by a plateau that remained until week 16. The fimbria-deficient mutant DPG3 did not bind antifimbrial antibody and was not opsonized, whereas strain 381, the parent of the mutant, was opsonized. The specific antibody bound to and opsonized P. gingivalis strains 33277 and 381 (fimbria type I) but not W50, A7A-1-28, 9-14K-1 or FAY-19M-1 (fimbrial types II-V). Specific antibody bound to strain 2561 (fimbrial type I) but, as assessed by chemiluminescence, did not opsonize it. While fimbriae have opsonic target sites that are accessible on P. gingivalis cell surfaces, the relevant opsonic target sites do not appear to be shared across serotypes or fimbrial types. Thus, a vaccine containing, as antigen, fimbrial protein from a single P. gingivalis strain would likely be ineffective against infections by P. gingivalis strains expressing other fimbrial types.
authors.affiliation: Department of Periodontics, School of Dentistry, University of Washington, Seattle WA 98195, USA.
authors.forename: Q
authors.initials: Q
authors.lastname: Fan
authors.forename: T
authors.initials: T
authors.lastname: Sims
authors.forename: H
authors.initials: H
authors.lastname: Sojar
authors.forename: R
authors.initials: R
authors.lastname: Genco
authors.forename: R C
authors.initials: RC
authors.lastname: Page
mesh_terms: D000818:Animals; D000907:Antibodies, Bacterial / Q000276:immunology*; D000937:Antigen-Antibody Reactions / Q000276:immunology; D000942:Antigens, Bacterial / Q000097:blood / Q000276:immunology; D000954:Antigens, Surface / Q000276:immunology; D001422:Bacterial Adhesion; D001428:Bacterial Vaccines / Q000276:immunology; D015153:Blotting, Western; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D010861:Fimbriae, Bacterial / Q000276:immunology*; D006801:Humans; D015151:Immunoblotting; D008163:Luminescent Measurements; D009154:Mutation / Q000235:genetics; D009504:Neutrophils / Q000276:immunology*; D009895:Opsonin Proteins / Q000276:immunology*; D010518:Periodontitis / Q000382:microbiology; D010587:Phagocytosis / Q000276:immunology*; D016966:Porphyromonas gingivalis / Q000145:classification / Q000235:genetics / Q000276:immunology*; D011817:Rabbits; D012703:Serotyping
chemical_list: D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001428:Bacterial Vaccines; D009895:Opsonin Proteins