Development of inhibitory peptide in oral bacterial coaggregation
| Project/Area Number |
09044302
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Field |
矯正・小児・社会系歯学
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| Research Institution | Osaka University |
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Principal Investigator |
SHIZUKUISHI Satoshi Osaka University, Faculty of Dentistry, Professor, 歯学部, 教授 (00028789)
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| Co-Investigator(Kenkyū-buntansha) |
SHARMA A State University of New York at Buffalo, Research associate, 助手
SOJAR H.T. State University of New York at Buffalo, Assistant professor, 助教授
GENCO R.J. State University of New York at Buffalo, Distinguished professor, 最上級教授
NAGATA Hideki Osaka University, Faculty of Dentistry, Assistant professor, 歯学部附属病院, 講師 (50260641)
AMANO Atsuo Osaka University, Faculty of Dentistry, Assistant professor, 歯学部附属病院, 講師 (50193024)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥4,500,000 (Direct Cost: ¥4,500,000)
Fiscal Year 1998: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1997: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | Periodontopathic bacteria / Porphyromonas gingivalis / Fimbriae / Coaggregation / Gram-positive bacteria / Streptococcus oralis / Salivary protein / Adherence / Streptococcus oralls |
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| Research Abstract |
The objects of this study are to determine the coadhesins which mediate coaggregation between Pomhyromonas gingivalis and oral gram-positive bacteria, and to develop inhibitory peptide in the coaggregation. Among various components of P.gingivalis, fimbriae strongly inhibited the coaggregation between P.gingivalis and Streptococcus oralis by the turbidimetric method. The inhibition studies using recombinant fimbrillin and synthetic peptides showed that amino acid residues 266-286 of fimbrillin contain a domain involved in the coaggregation. Previously, we reported that this domain mediates the binding of P.gingivalis to praline-rich protein (REP) and statherin. Therefore, this peptide may acy as an effective inhibitor against P.gingivalis adherence. We also reported that the carboxyl-terminal fragment of PRP is responsible for the REP-binding to P.gingivalis. In this study, we found that this fragment inhibited P.gingivalis adherence to plaque-forming gram-positive bacteria as well as
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to PRP.This fragment also appears to be one of the potent coaggregation-inhibitory peptides. To identify the coadhesin from gram-positive bacteria, the interactions of surface components from S.oralis with P.gingivalis flmbriae were examined. 35-kDa S.orals surface component reacted with P.gingivalis fimbriae. The partial purified 35-kDa protein inhibited the coaggregation between P.gingivalis and S.oralls. The antibodies against 35-kDa protein reacted with Streptococcus sanguis and Streptococcus gordonii, indicating that the similar proteins related to 35-kDa S.oralis surface protein exsit in various oral gram-positive bacteria. They also seems to play an important role in the coaggregation. Further identification of the P.gingivalis binding region in the 35-kDa protein is in progress. In-this study, we obtained several peptides which inhibit P.gingivalls adherence to gram-positive bacteria. Although further evaluation of these peptides are necessary, they may be avairable to prevent P.gingivalls adherence to dental plaque. Less
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Report
(3 results)
Research Products
(5 results)
