| Project/Area Number |
18310141
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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 |
Living organism molecular science
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| Research Institution | Hokkaido University |
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Principal Investigator |
TANAKA Isao Hokkaido University, Fac. of Adv. Life Sci., Prof. (70093052)
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| Co-Investigator(Kenkyū-buntansha) |
WATANABE Nobuhisa Hokkaido Univ., Fac. of Adv. Life Sci., Assoc. Prof. (70212321)
YAO Min Hokkaido Univ., Fac. of Adv. Life Sci., Assoc. Prof. (40311518)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥18,070,000 (Direct Cost: ¥16,000,000、Indirect Cost: ¥2,070,000)
Fiscal Year 2007: ¥8,970,000 (Direct Cost: ¥6,900,000、Indirect Cost: ¥2,070,000)
Fiscal Year 2006: ¥9,100,000 (Direct Cost: ¥9,100,000)
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| Keywords | Staphylococcus aureus / Cell-wall associated protein / Adhesion mechanism / X-ray structure analysis / Binding protein |
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| Research Abstract |
This research focused on the protein involved in the adhesion of Staphylococcus aureus to the host cell. The final goal of this research is to understand the adhesion mechanism of this bacterium to the host cell and to establish the structural basis for the drug design. During the project period, the structure of a giant protein EbhA, which was thought to be involved in the endocarditis, was investigated by the X-ray crystallography, small angle X-ray scattering, CD spectroscopy and electron microscopy. First, we elucidated the structure of the two repeating units (Ebh-R7-R8) of this molecule by the X-ray crystallography. Then, based on the studies of the small angle X-ray scattering and CD spectrometry, we proposed that these structures are connected tandem. Furthermore, the electron microscopy showed that the Ebh-R10-19 is the string of about 500A in length which is consistent with the proposed structure. Finally, we simulated the whole Ebh structure by calculating the helical parameters of this molecule based on the X-ray structure, which showed that Ebh is the string of about 3200 A in length. These studies suggest that Ebh is on the surface of the Staphylococcus aureus cell and plays the role as "skeleton molecule" to reinforce the cell.
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