Analysis of functional and physical HN-F interaction in the course of membrane fusion by paramyxoviruses
Project/Area Number |
26460552
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Virology
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Research Institution | Mie University |
Principal Investigator |
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Project Period (FY) |
2014-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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Keywords | パラインフルエンザウイルス / HN蛋白 / F蛋白 / 分子間相互作用 / 膜融合 / 細胞融合 |
Outline of Final Research Achievements |
It is widely appreciated that during the course of membrane fusion by parainfluenza viruses, the head domain of the viral envelope protein HN (hemagglutinin-neuraminidase) undergoes a structural transition after its binding to the receptors on the cell surface, that exposes otherwise hidden stalk domain of the HN. The exposed HN stalk domain then interacts with the head domain of another viral envelope protein F (fusion) in a virus-specific manner, which enables the F to undergo a series of structural changes that lead to merger of viral and cellular membranes. Such specificity is believed to be defined by the similarity in the primary structures of the HN stalk domain and the F head domain between different viruses. However, our present study revealed that the HN head domain and F stalk domain can modulate the specificity by affecting tertiary and/or quaternary structures of the HN stalk domain and the F head domain, respectively.
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Report
(4 results)
Research Products
(24 results)
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[Journal Article] Inhibition of human parainfluenza virus type 2 growth in vitro by catechin is caused by the inhibition of genome and mRNA synthesis and by the disruption of cytoskeleton, and that by tannic acid is mainly caused by genome synthesis inhibition and the disruption of cytoskeleton2014
Author(s)
Uematsu J, Kihira S, Uchida M, Sakakura Y, Deguchi S, Sakai K, Yamamoto H, Kawano M, Tsurudome M, O'Brien M, Komada H
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Journal Title
International Journal of Sciences
Volume: 3
Pages: 47-55
Related Report
Peer Reviewed
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[Journal Article] Ribavirin inhibits human parainfluenza virus type 2 replication in vitro.2014
Author(s)
Kihira S, Uematsu J, Kawano M, Itoh A, Ookohchi A, Satoh S, Maeda Y, Sakai K, Yamamoto H, Tsurudome M, O'Brien M, Komada H.
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Journal Title
Microbiol Immunol.
Volume: 58
Issue: 11
Pages: 628-635
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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