| Project/Area Number |
13470063
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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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 | Tokyo Institute of Technology |
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Principal Investigator |
HANADA Hiroshi Tokyo Institute of Technology, Frontier Collaborative Research Center, Professor, フロンティア創造共同研究センター, 教授 (80107432)
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| Co-Investigator(Kenkyū-buntansha) |
ARISAKA Fumio Tokyo Institute of Technology, Graduate School of Biosciense and Biotechnology, Associate Professor, 大学院・生命理工学研究科, 助教授 (80133768)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥13,800,000 (Direct Cost: ¥13,800,000)
Fiscal Year 2002: ¥5,600,000 (Direct Cost: ¥5,600,000)
Fiscal Year 2001: ¥8,200,000 (Direct Cost: ¥8,200,000)
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| Keywords | SV40 / AAV / capsid protein / virus-like particle / recombinant plasmid / nano-machine |
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| Research Abstract |
The siman virus 40 (SV40) capsid is composed of 72 pentamers of its major protein, VP1, that are arranged in a icosahedral surface lattice. This structure is maintained by appropriately arranged three types of non-equivalent interactions between the pentamers. However, it remains unclear how these interactions are achieved. We analyzed the in vitro assembly of recombinant VP1. Electron microscopic observations revealed that these VP1s assembled into structurally divergent particles depending on the conditions. The VP1 pentamers efficiently assembled into virus-like particles (VLPs) when high ammonium sulfate concentrations are present. In the presence of Ca2+ at neutral pH, the VP1 pentamers formed not only VLPs but also produced tiny icosahedral particles and tubular structures. Exclusion of Ca2+ resulted in the exclusive formation of the tiny particles. In contrast, at pH 5, the VP1 pentamers produced only extraordinarily long tubular structures. VP1 is thus quite unique in htat it can assemble into such diverse structures, and the assembly properties of SV40 VP1 are clearly different from those of previously reported murine polyoma virus VP1. These observations provide clues that will help elucidate the mechanisms underlying SV40 capsid formation. Moreover, that particular conditions promote the selective assembly of VP1 into different particle structures suggests that we can alter the shapes and sizes of the aritifical SV40 capsids used to deliver drugs or genes.
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