| Project/Area Number |
14570257
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | National Institute of Infectious Diseases |
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Principal Investigator |
WATANABE Haruo National Institute of Infectious Diseases, Department of Bacteriology, Director, 細菌第一部, 部長 (70142130)
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| Co-Investigator(Kenkyū-buntansha) |
HIROSE Kenji National Institute of Infectious Diseases, Department of Bacteriology, Chief, 細菌第一部, 主任研究員 (70311397)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2003: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2002: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Shigella / cell invasion / phagocytosis / IpaC / effector molecule / actin / β-catenin / 貧食 / ベーター・カテニン |
|---|
| Research Abstract |
IpaC of Shigella is essential for initial bacterial entry into epithelial cells. We report that IpaC interacts with β-catenin and destabilizes the cadherin-mediated cell adhesion complex. Using a yeast two-hybrid system, we identified β-catenin as a binding partner of IpaC within the host cell after cell entry, but not in the initial entry. Co-immunoprecipitation, confocal microscopy, and GST pull down experiments confirmed the intracellular and cell-free interactions between these two proteins. The interaction sites were mapped to the ninth armadillo repeat of β-catenin and to the C-terminus of IpaC. IpaC-associated β-catenin was phosphorylated at tyrosine residues. This phosphorylation led to the destabilization of the functional cadherin-catenin complex, which could be a mechanism whereby the epithelial cell-cell tight adhesion is disrupted. These events may facilitate the further basolateral invasion of bacteria through the disrupted space and/or modulate the cell-to-cell spread of Shigella.
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