2020 Fiscal Year Final Research Report
Structural basis for the mechanism of bacterial type III secretion system by CryoEM
Project/Area Number |
17K07365
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Osaka University (2018-2020) Institute of Physical and Chemical Research (2017) |
Principal Investigator |
Fujii Takashi 大阪大学, 生命機能研究科, 特任准教授(常勤) (10582611)
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Project Period (FY) |
2017-04-01 – 2021-03-31
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Keywords | クライオ電顕 |
Outline of Final Research Achievements |
Dysentery bacteria use the type III secretion system called needle complex to launch effector proteins into host cells, inducing phagocytosis with restructuring of the host cytoskeleton, which is then used to invade and infect host cells. The needle complex can be divided into a membrane-spanning basal body, a needle and a tip complex, which is the tip of the needle. Interestingly, there are several mutant strains that differ in the pattern of toxin secretion in the needle component protein MxiH, rather than in the base, which is a transport gate, or in the tip complex, which is in direct contact with host cells. In this research project, we analyzed the mutants using cryo-electron microscopy to elucidate the structural biological basis of the bacterial toxin secretion mechanism.
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Free Research Field |
生物物理
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Academic Significance and Societal Importance of the Research Achievements |
貧困国を中心として、赤痢菌による細菌感染症は多くの生命を奪う深刻な問題である。赤痢菌の毒素蛋白質輸送機構のメカニズムを原子レベルの構造解析によって可視化することは、そのメカニズムの解明への大きな一歩となる。輸送ゲートや宿主細胞に直接結合するチップ複合体についての変異ではくニードルと呼ばれる繊維構造(毒針部分)への変異が毒素分泌パターンに大きな違いをうむことは非常に興味深い。この謎にクライオ電顕で迫った。
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