The analysis of functional domains of NS1 protein involved in the regulation of influenza C virus replication
| Project/Area Number |
23590536
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Yamagata University |
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Principal Investigator |
HONGO SEIJI 山形大学, 医学部, 教授 (90229245)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMOTAI Yoshitaka 山形大学, 医学部, 助教 (30445746)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | C型インフルエンザ / ウイルス / NS1 / スプライシング / 核移行シグナル / 核外移行シグナル / 増殖 / splicing / influenza C virus / 病原性 |
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| Research Abstract |
To investigate the mechanism by which influenza C virus NS1 protein can up-regulate splicing, we tried to find the nuclear localization signal of NS1. The C-terminal deletion mutants of NS1 were expressed in COS-1 cells and the intracellular localization of the expressed mutants was analyzed by immunofluorescence. The wild type NS1 composed of residues 1-246 and C-terminal deletion mutant of residues 1-154 were localized in the cytoplasm predominantly. However, C-terminal deletion mutant of residues 1-108 was localized in the nucleus and cytoplasm. These results suggest that nuclear export signal of NS1 may be present between residues 109 and 154.
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Report
(4 results)
Research Products
(43 results)
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[Journal Article] Molecular epidemiology of Coxsackievirus A16 strains isolated from children in Yamagata, Japan between 1988 and 2011.2013
Author(s)
Mizuta K, Abiko C, Aoki Y, Ikeda T, Matsuzaki Y, Hongo S, Itagaki T, Katsushima N, Ohmi A, Nishimura H, Ahiko T.
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Journal Title
Microbiol Immunol.
Volume: 57
Issue: 5
Pages: 400-405
DOI
Related Report
Peer Reviewed
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