2016 Fiscal Year Final Research Report
structural study of the ebola virus proteins
Project/Area Number |
15K21272
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
Virology
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Research Institution | Yokohama City University |
Principal Investigator |
sugiyama kanako 横浜市立大学, 生命医科学研究科, 客員研究員 (20623226)
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Project Period (FY) |
2015-04-01 – 2017-03-31
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Keywords | エボラウイルス / ウイルスタンパク質 / 構造解析 |
Outline of Final Research Achievements |
Ebola virus cause ebola disease. Interaction between some viral proteins like RNA polymerase(RNAP), Nucleoprotein(NP), VP30 and VP35 is important for viral life. To clarify the relationship between proteins, I tried to solve the structure. Which domain or amino acid affect at interaction area was unknown. So I expressed viral protein in E.coli, and obtained the peptide, RNAP1-466,551-904,1187-1650,NP25-420(1),420-730(2),630-739(3),VP30N,VP30C,VP35N and VP35C. The peptide of RNAP is unstable and couldn’t analysis interaction. NP1 and VP35N, NP2 and VP30C, NP2 and VP35C bind each other. But under the crystallization condition, complex was divided. Then I confirmed the detail of amino acid at the interaction area. But in 2015 and 2016, the structure of NP1-VP35N and NP2-VP30C was reported by other group. In the reports, the importance of relationship was shown. The interaction between RNAP and viral proteins is unknown, yet. It may lead more knowledge about ebola virus and ebola disease.
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Free Research Field |
ウイルスタンパク質の構造解析
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