| Project/Area Number |
25670066
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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 |
Environmental and hygienic pharmacy
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| Research Institution | Tokyo Metropolitan Institute of Medical Science |
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Principal Investigator |
KAJIWARA Naoki 公益財団法人東京都医学総合研究所, ゲノム医科学研究分野, 主任研究員 (70453917)
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| Co-Investigator(Renkei-kenkyūsha) |
SHIBASAKI Futoshi 公益財団法人東京都医学総合研究所, ゲノム医科学研究分野, プロジェクトリーダー (90300954)
NOMURA Namiko 公益財団法人東京都医学総合研究所, ゲノム医科学研究分野, 主任基盤技術研究職員 (50599694)
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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| Keywords | インフルエンザ / H5N1 / 感染 / 高病原性 / 肺炎 / ヘマグルチニン / シアル酸 |
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| Outline of Final Research Achievements |
Outbreak of influenza virus poses serious threats to public health worldwide. In recent years, highly pathogenic avian influenza A virus H5N1 has caused fatal human infection in Asia and many other countries, increasing fears of human pandemic. However, it remains to be elucidated how avian viruses acquire the ability to infect humans. Hemagglutinin (HA) is responsible for the binding of virus to cell surface and the subsequent fusion event. In contrast to low pathogenic viruses, highly pathogenic ones contain multiple basic amino acids at cleavage site of HA protein. We found that this unique motif might contribute to human infection with highly pathogenic H5N1 virus because the cluster of basic amino acid such as TAT peptide and poly-arginine functions as cell penetrating peptide. Our findings suggest that the unique motif at HA cleavage site of highly pathogenic H5N1 virus has the potential to enter cells via binding to some protein on plasma membrane.
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