IMPORTANCE OF LEUCINE ZIPPER-LIKE DOMAIN OF RIFT VALLEY FEVER VIRUS L PROTEIN FOR VIRAL RNA SYNTHESIS
| Project/Area Number |
23780314
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Applied veterinary science
|
|---|
| Research Institution | National Institute of Infectious Diseases |
|---|
Principal Investigator |
AYA NIIKURA 国立感染症研究所, 動物管理室, 研究員 (10392325)
|
|---|
| Project Period (FY) |
2011 – 2012
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
|
|---|
| Keywords | リフトバレー熱ウイルス / RNA複製機構 / L蛋白 / RNAポリメラーゼ / RiftValleyFever virus |
|---|
| Research Abstract |
Rift Valley fever virus (RVFV) (genus Phlebovirus, family Bunyaviridae) causes mosquito-borne endemic and epidemic diseases among humans and livestock. The virus carries three RNA segments, L, M and S. The L RNA encodes L protein, an RNA-dependent RNA polymerase and a RVFV L oligomer, together with N, which is encoded by the S RNA, exerts viral RNA synthesis. Although RVFV L encodes conserved domains among other segmented RNA viruses, the functional domains of RVFV L have not yet been characterized. The N-terminus region of L contained a leucine zipper-like domain, in which leucine residues repeat 4 times at every 7th position. By mutational analysis combined with minigenome assay, Co-immunoprecipitation or Bi-molecular Fluorescence assay (BiFC), we demonstrated that the leucine zipper-like domain was important for intramolecular interaction with C-terminus to exert viral RNA synthesis.
|
Report
(4 results)
Research Products
(3 results)
