Characterization of the outer membrane protein complex in the Por secretion pathway
Project/Area Number |
23592715
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Morphological basic dentistry
|
Research Institution | The Nippon Dental University |
Principal Investigator |
SAIKI Keitarou 日本歯科大学, 生命歯学部, 講師 (30297973)
|
Project Period (FY) |
2011-04-28 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
|
Keywords | 歯周病 / タンパク分泌 / 歯周炎 / タンパク質分泌 / 慢性歯周炎 |
Outline of Final Research Achievements |
Porphyromonas gingivalis, the etiologic agent of chronic periodontitis, secretes C-terminal domain (CTD) proteins, which are involved in virulence and proliferation of this bacterium, via the Por secretion pathway (PorSP). PorSP is composed of steps such as passage through the outer membrane via the CTD-dependent Por secretion system (PorSS), cleavage of their CTDs by the CTD signal peptidase PG0026, glycolipid-conjugation, and anchorage to the outer cell membrane and/or the extracellular vesicles. PG0026 is one of the CTD proteins and secreted via PorSS, but undergoes no successive modifications. In this study, I found that PG0026 anchors to the cell surface by interacting with outer membrane protein PG27 that is involved in the glycolipid modification of CTD proteins, and functions in processing of other CTD proteins such as gingipains. This study also demonstrates the complex formation of the outer membrane proteins in PorSP.
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Report
(5 results)
Research Products
(8 results)