| Project/Area Number |
25462894
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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 |
Functional basic dentistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
OHARA-NEMOTO Yuko 長崎大学, 医歯薬学総合研究科(歯学系), 准教授 (10164667)
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| Co-Investigator(Kenkyū-buntansha) |
NEMOTO Takayuki K. 長崎大学, 医歯薬学総合研究科(歯学系), 教授 (90164665)
KIMURA Shigenobu 岩手医科大学, 歯学部, 教授 (10177917)
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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: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | Porphyromonas gingivalis / ジペプチジルペプチダーゼ / アミノ酸代謝 / ペリプラズム / 歯周病 / ペプチダーゼ / 歯周病原性細菌 / 嫌気性菌 / 糖非発酵性細菌 / 口腔細菌 / 酵素 |
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| Outline of Final Research Achievements |
We examined enzymatic activity and cellular localization of a group of dipeptidyl peptidases (DPP) in a periodontopathic bacterium, Porphyromonas gingivalis. This study revealed that DPP5, which had been discovered in fungi, was expressed in the bacterium, and that a novel peptidase, acylpeptidyl oligopeptidase (AOP), was identified. Ortholog search demonstrated wide spreading of the two exopeptidases from bacteria, archea to eukaryote. DPP5 cleaves X-Ala dipeptides from the N-terminus of oligopeptides and AOP liberates di- and tri-peptides from N-terminally blocked ones. Both peptidases were expressed in the periplasmic space of the bacterium. Consequently, we proposed that dipeptide-producing exopeptidases including DPP4, DPP5, DPP7, DPP11 and AOP are crucial for the growth and pathogenicity of P. gingivalis.
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