| Project/Area Number |
15K14859
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Veterinary medical science
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| Research Institution | Institute of Physical and Chemical Research |
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Principal Investigator |
Ogawa Kenji 国立研究開発法人理化学研究所, 吉田化学遺伝学研究室, 専任研究員 (50251418)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 人獣共通感染症 |
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| Outline of Final Research Achievements |
Rabies virus phosphoprotein (P protein) play an important role in the virus replication and suppression of host immunity. We focused on the P protein as a drug target, and established assay for measuring (1) P protein dimerization, and the interaction between the P protein and (2) rabies virus nucleoprotein and (3) host dynein L chain based on the split-luciferase complementation assays. The assays can be adapted to a high-throughput format to identify novel anti-rabies virus compounds. We next examined the relationship between the dimerization and immunosuppressive activity of P protein. The split-luciferase assay and Western blotting revealed that a mutant P protein in which Tyr-128 was substituted with Ala (Y128A) was defective in dimerization. However, the Y128A mutant P protein has the immunosuppressive activity comparable to the wild-type P protein. Thus, different functional domains of the P protein may be responsible for the dimerization and immunosuppressive activity.
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