| Project/Area Number |
12672040
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Periodontal dentistry
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| Research Institution | Keio University (2002)
Tokyo Dental College (2000-2001) |
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Principal Investigator |
NAKAGAWA Taneaki Keio University, School of Medicine, Professor, 医学部, 教授 (00227745)
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| Co-Investigator(Kenkyū-buntansha) |
ISHIHARA Kazuyuki Tokyo Dental College, AssociateProfessor, 歯学部, 助教授 (00212910)
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| Project Period (FY) |
2000 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2002: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2001: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2000: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | Porphyromonas gingivalis / gingipains / opsonization / Kgp / Rgp / ケミルミネッセンス法 / 免疫応答 |
|---|
| Research Abstract |
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
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