Study of localization mechanism of cell surface proteins in Porphyromonas gingivalis
| Project/Area Number |
25462863
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Morphological basic dentistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
SHOJI Mikio 長崎大学, 医歯薬学総合研究科(歯学系), 助教 (10336175)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 歯周病細菌 / リポ多糖 / 歯周病菌 / LPS |
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| Outline of Final Research Achievements |
The periodontal pathogen Porphyromonas gingivalis has approximately 30 proteins (called CTD proteins) that contain a conserved C-terminal domain. We have reported that CTD proteins are secreted onto the cell surface via the Type IX secretion system, and some of CTD proteins are anchored on the cell surface by binding to A-LPS. However, the mechanism of A-LPS biosynthesis remains to be determined.
In this study, we found that WzzP, Wzx, WbaP, PGN_0002 are involved in the A-LPS biosynthesis.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Identification of an O-antigen chain length regul tor, WzzP, in Porphyromonas gingivalis.2013
Author(s)
Shoji M, Yukitake H, Sato K, Shibata Y, Naito M, Aduse-Opoku J, Abiko Y, Curtis MA, N kayama K.
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Journal Title
Microbiologyopen.Epub
Volume: 10
Issue: 3
Pages: 383-401
DOI
Related Report
Peer Reviewed
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