| Project/Area Number |
20780217
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Applied veterinary science
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
NODA Takeshi The University of Tokyo, 医科学研究所, 特任助教 (00422410)
|
|---|
| Project Period (FY) |
2008 – 2009
|
| Project Status |
Completed (Fiscal Year 2009)
|
| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
|
|---|
| Keywords | 人獣共通感染症 / エボラウイルス / ヌクレオカプシド / 電子顕微鏡 / エポラウイルス / nucleopTotein / 電子顕微鏡解析 |
|---|
| Research Abstract |
When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures. Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA which is not protected from RNase digestion and that the morphology of the helix changes depending on the environmental salt concentration. The N-terminal 450 amino acid residues of NP are sufficient for these properties. However, digestion of the NP-associated RNA eliminates the plasticity of the helix, suggesting that this RNA is an essential structural component of the helix, binding to individual NP molecules via the N-terminal 450 amino acids. These findings enhance our knowledge of Ebola virus assembly and understanding of the Ebola virus life cycle.
|
