The analysis of the immune response to the virulence factors of the periodontopathic bacteria

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We initiated a study to determine whether RgpA and Kgp have opsonic target sites and whether these sites are available and accessible on intact P.gingivalis cells. Rabbits were immunized and IgG fractions were isolated from preimmune and immune sera. Functional characteristics of the antibodies were assessed by determining antibody titers by ELISA, generating Western blots, and measuring of the antibody enhancement of P.gingivalis opsonization, phagocytosis and killing by polymorphonuclear leukocytes of intact cells of P.gingivalis representative of the four serotypes. Both RgpA and Kgp induced high titers of IgG antibody. Anti-RgpA and anti-Kgp antibody bound to both RgpA and Kgp demonstrating a large proportion of shared antigenic epitopes. The two antibodies bound equally well to all four P.gingivalis serotypes compared to preimmune IgG. The immunoblot patterns of binding of the two antibodies to RgpA and Kgp and to sonlcates of the four P.gingivalis serotypes were virtually identical. Both proteins induced antibodies that significantly enhanced opsonization as assessed by chemiluminescence. Both antibodies significantly enhanced PMN-mediated bacterial killing of the four P.gingivalis serotypes. These data indicate these two proteins appear to be potential candidate antigens for an anti-P.gingivalis vaccine. We have similar data on RgpB, which possesses only a catalytic domain. The data indicate that RgpB also appear to be potential candidate antigen for anti-P.gingivalis vaccine