2016 Fiscal Year Final Research Report
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 |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Mie University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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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 |
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| 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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| Free Research Field |
ウイルス学・分子生物学
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