2007 Fiscal Year Final Research Report Summary
Elucidation of molecular mechanism on periodontal bacterial adherence, invasion and signal transduction to human cell
| Project/Area Number |
18390567
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Social dentistry
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| Research Institution | Osaka University |
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Principal Investigator |
NAGATA Hideki Osaka University, Graduate School of Dentistry, Associate Professor (50260641)
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| Co-Investigator(Kenkyū-buntansha) |
SHIZUKUISHI Satoshi Osaka University, Graduate School of Dentistry, Professor (00028789)
KATAOKA Kosuke Osaka University, Graduate School of Dentistry, Assistant Professor (50283792)
KUBONIWA Masae Osaka University, Graduate School of Dentistry, Assistant Professor (00303983)
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| Project Period (FY) |
2006 – 2007
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| Keywords | periodontopathic bacteria / human gingival fibroblast / GAPDH / fimhriae / adherence / invasion |
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| Research Abstract |
In this study, we demonstrated that interaction between human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Porphyromonas gingivalis fimhrise was specific and high affinity via a biomolecolar interaction analysis system (BIAcore). Human GAPDH was digested with various proteinasas such as lysylendopeptidase and fragments were collected by HPLC. Binding activity of each GAPDH fragment to P. gingivalis fimbriae was measured via BIAcore, and the fragment which demonstrated the strongest binding activity was analyzed with mass spectrometer and amino acid sequencer. Since it was found that the binding domain for P. gingivalis fimbriae existed in amino acid residues 165-185 of human GAPDH, we synthesized the peptide corresponding to amino acid residues 165-185 of human GAPDH, and examined the inhibitory effect of the peptide on P. gingivalis adherence and invasion to human gingival fibroblast with confocal microscpe. The synthetic peptide inhibited P. gingivalis adherence and invasion to human fibroblast in a dose-dependent manner. Next, we identified the binding domain of Streptococcus oralis GAPDH for P. gingivalis fimbriae by the same method as we described above, and found that the fimbrial binding domain of S oralis GPADH existed in the same region as that of human GAPDH. Therefore, we investigated the inhibitory effect of the synthetic peptide corresponding to P. gingivalis fimbriae-binding region on biofilim formation of P. gingivalis with S. oralis. The peptide also inhibited P. gingivalis S. oralis biofilm formation in a dose-dependent manner.
In conclusion, the synthetic peptide corresponding to P. gingivalis fimbriae-binding region inhibited P. gingivalis biofilm formation and P. gingivalis adherence and invasion to human fibroblast, indicating that the peptide might be a potent preventive against periodontitis.
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Research Products
(16 results)
