Fimbriae of Porphyromonas gingivalis induce opsonic antibodies that significantly enhance phagocytosis and killing by human polymorphonuclear leukocytes
Q. Fan et al., Fimbriae of Porphyromonas gingivalis induce opsonic antibodies that significantly enhance phagocytosis and killing by human polymorphonuclear leukocytes, ORAL MICROB, 16(3), 2001, pp. 144-152
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 d
etermine whether P. gingivalis fimbriae have opsonic target sites and wheth
er they are accessible on the cell surfaces and cross-reactive among P. gin
givalis fimbral types and serotypes. Rabbits were immunized with a vaccine.
The antiserum reacted with a 43-kDa fimbrillin monomer and a 43-kDa compon
ent 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 soni
cate of strain DPG3, a mutant that does not express functional fimbriae. Th
e antibody enhanced chemiluminescence approximately six-fold relative to pr
eimmune serum values and significantly enhanced phagocytosis and killing of
P. gingivalis 33277 by human polymorphonuclear leukocytes. Peak opsonic ac
tivity was observed at week 6 followed by a plateau that remained until wee
k 16. The fimbria-deficient mutant DPG3 did not bind antifimbrial antibody
and was not opsonized, whereas strain 381, the parent of the mutant, was op
sonized. 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 ty
pe I) but, as assessed by chemiluminescence, did not opsonize it. While fim
briae have opsonic target sites that are accessible on P. gingivalis cell s
urfaces, the relevant opsonic target sites do not appear to be shared acros
s serotypes or fimbrial types. Thus, a vaccine containing, as antigen, fimb
rial protein from a single P. gingivalis strain would likely be ineffective
against infections by P, gingivalis strains expressing other fimbrial type
s.