Study of relationship of physiological roles and pathogenicity of aggressive periodontopathic bacterial quinol peroxidase
Project/Area Number |
21592346
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Morphological basic dentistry
|
Research Institution | The Nippon Dental University |
Principal Investigator |
|
Project Period (FY) |
2009 – 2012
|
Project Status |
Completed (Fiscal Year 2012)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2012: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2011: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
|
Keywords | 口腔細菌学 / ペルオキシダーゼ / 呼吸鎖 / 侵襲性歯周炎 / 蛋白質 / 歯学 / 微生物 / 感染症 / 細菌 |
Research Abstract |
Quinol peroxidase (QPO) of Aggregatibacter actinomycetemcomitans catalyzes peroxidase activity using a quinol on respiratory chain.Aqpo null mutant exhibits an oxidative stress phenotype, suggesting that QPO plays animportant role in scavenging endogenously generated hydrogen peroxide, and exhibitsreduced production of leukocyte (LtxA), a secreted bacterial toxin that is known to targethuman leukocytes. Screening identified ascofuranone as a highly potent inhibitor of QPO(Ki = 9.6 nM). This inhibitor also reduced the secretion of LtxA, with an associatedreduction in the pathogenicity ofA. actinomycetemcomitans for HL-60 cells. We producedthe recombinant QPO expression system inEscherichia coli. Purified recombinant QPOwas used to analyse the catalytic mechanism, indicating that QPO catalyzes as ping pongbi bi mechanism.
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Report
(5 results)
Research Products
(14 results)