| Project/Area Number |
21790846
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neurology
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| Research Institution | Nagasaki University |
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Principal Investigator |
SANO Kazunori Nagasaki University, 大学院・医歯薬学総合研究科, 助教 (50534343)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2010: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 神経分子病態学 / プリオン / リコンビナントプリオンタンパク / アミロイド / 構造 / 感染 / プリオン病 / 立体構造 / 感染性 |
|---|
| Research Abstract |
Recently, we developed an in vitro recombinant PrP (recPrP) conversion system with shaking (Quaking-Induced Conversion ; QUIC). We generated recPrP-amyloid in vitro by the tiny amounts of mouse brain homogenates with Chandler and 22L strains using this system. The shape of β-sheet spectrum by infrared spectroscopy in these recPrP-amyloids was similar to that of PrP^<Sc> isolated from each infectious brain, and unique to the strains. Additionally, the conformational stability analysis using denaturation by guanidine-hydrochloride demonstrated that the stability of recPrP-amyloid was similar to that of PrP^<Sc> in brains, indicating that prion strain specific conformations are seemed to be conserved. To determine infectivity of recPrP amyloids, recPrP amyloids was inoculated intracerebrally into wild-type mice. recPrP amyloids significantly accelerated the onset of disease. These results suggest that prion strain-specific conformations are transmitted to recPrP-amyloid, which is PrP^<Sc>-like infectious agents.
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