| Project/Area Number |
14570270
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | University of Shizuoka |
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Principal Investigator |
SUZUKI Takashi University of Shizuoka, School of Pharmaceutical Sciences, Associate Professor, 薬学部, 助教授 (20240947)
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| Co-Investigator(Kenkyū-buntansha) |
IKEDA Kiyoshi University of Shizuoka, School of Pharmaceutical Sciences, Associate Professor, 薬学部, 助教授 (40168125)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2003: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2002: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | human parainflvenza / HN glycoprotein / analogs of sialic acid / sialidase / sialo sugar chain / receptor / HNタンパク質 / シアリダーゼ活性 |
|---|
| Research Abstract |
We demonstrated that 4-Ο-thiocarbamoylmethyl-Neu5Ac2en had strong inhibitory activity toward human parainfluenza type 1 (hPIV-1) sialidase. 4-Ο-thiocarbamoylmethyl-Neu5Ac2en was effective in inhibiting receptor binding and the growth of hPIV-1. To identify the region of the receptor binding pocket between hPIV-1 and hPIV-3, we generated the plasmid expression vector containing each hemagglutinin-neuraminidase gene. We found that hPIV-1 and hPIV-3 NHs had different receptor specificities. We evaluated the abilities of hPIV-1 and hPIV-3 to bind to different types of sialylglycoproteins, and we compared their binding abilities with that of SV. hPIV-1 and hPIV-3 preferentially bound to GP-2 with a terminal Neu5Ac linked to branched N-acetyllactosaminoglycans by the α2-3 linkage. hPIV-3 also weakly bound to glycoconjugates with a terminal Neu5Ac linked to branched N-acetyllactosaminoglycans by the α2-6 linkage. We also designed novel Neu5Ac2en analogs modified at the C-4 containing the different length of thioamido groups. We will analyze the effects of the analogs for hPIV-1 and hPIV-3 sialidase activities and the viral replication.
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