High resolution structure analysis of Porphyromonas gingivalis membrane proteins in the biofilm.
Project/Area Number |
22792114
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Social dentistry
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Research Institution | Osaka University |
Principal Investigator |
MAEDA Kazuhiko 大阪大学, 大学院・歯学研究科, 助教 (00346165)
|
Project Period (FY) |
2010 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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Keywords | 予防歯科学 / 歯周病 / Porphyromonas gingivalis / 口腔レンサ球菌 / プロテオーム / バイオフィルム / Prophyromonas gingivalis / 膜タンパク質 / GAPDH |
Research Abstract |
The purpose of this study is to identify and characterize new Porphyromonas gingivalis components that interact with Streptococcus oralis GAPDH. Pull-down assay was performed to detect potential interactions between P. gingivalis client proteins and S. oralis recombinant GAPDH. The proteins were separated by 2D-gel electrophoresis, and the five proteins ; RagA4, AbfD, GAPDH, GDH and MDH were identified by a proteomic-tandem mass spectrometry. Interaction between these P. gingivalis client proteins and S. oralis GAPDH was analyzed via a biomolecular interaction analysis system. S. oralis GAPDH demonstrated high affinity with five client proteins. Coaggregation between P. gingivalis and S. oralis was measured by turbidimetric method and fluorescence microscope. Recombinant RagA4, AbfD and GDH enhanced the coaggregation, whereas recombinant GAPDH and MDH inhibited in a dose-dependent manner. Furthermore, recombinant RagA4, AbfD and GDH regulated expression of luxS in P. gingivalis. These results indicate that five client membrane proteins of P. gingivalis might be regulators in P. gingivalis biofilm formation with oral streptococci.
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Report
(3 results)
Research Products
(5 results)