Role of multifunctional protein, GAPDH, associated with bacteria and human cells in infection by periodontopathic bacteria
Project/Area Number |
20390534
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Social dentistry
|
Research Institution | Osaka University |
Principal Investigator |
NAGATA Hideki Osaka University, 大学院・歯学研究科, 准教授 (50260641)
|
Co-Investigator(Kenkyū-buntansha) |
KUBONIWA Masae 大阪大学, 大学院・歯学研究科, 助教 (00303983)
MAEDA Kazuhiko 大阪大学, 大学院・歯学研究科, 助教 (00346165)
|
Co-Investigator(Renkei-kenkyūsha) |
KATAOKA Kosuke 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 准教授 (50283792)
|
Project Period (FY) |
2008 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥19,110,000 (Direct Cost: ¥14,700,000、Indirect Cost: ¥4,410,000)
Fiscal Year 2010: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2009: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
Fiscal Year 2008: ¥8,320,000 (Direct Cost: ¥6,400,000、Indirect Cost: ¥1,920,000)
|
Keywords | GAPDH / 歯周病細菌 / ヒト細胞 / 感染 / 付着 |
Research Abstract |
This study showed that a binding domain for P. gingivalis fimbriae may exist within amino acid residues 166 to 183 of S. oralis ATCC 9811 GAPDH. The peptide corresponding to amino acid residues 166 to 183 of S. oralis ATCC 9811 GAPDH (pep166-183) inhibited the interbacterial biofilm formation by several oral streptococci and P. gingivalis strains with different types of FimA. pep166-183 strongly inhibited biofilm formation between P. gingivalis and several oral bacteria which showed relatively strong cell surface-associated GAPDH activity. Moreover, we found that the binding domain for P. gingivalis fimbriae in human cell GAPDH may exist within the same domain as in S. oralis GAPDH.
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Report
(4 results)
Research Products
(44 results)