| Project/Area Number |
07670309
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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 | Osaka University |
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Principal Investigator |
YOH Myonsun Biken Osaka Univ.Res.Assoc., 微生物病研究所, 助手 (70093482)
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| Co-Investigator(Kenkyū-buntansha) |
IIDA Tetsuya Biken.Osaka Univ.Res.Assoc., 微生物病研究所, 助手 (90221746)
HONDA Takeshi Biken.Osaka Univ.Prof., 微生物病研究所, 教授 (60029808)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1996: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1995: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Vibrio parahaemolyticus / TDH / Biochemical study / Pathogenesis / Hemolysis / Phosphorylation |
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| Research Abstract |
We performed this study to make clear the mechanism of hemolysis induced by Vibrio parahaemolyticus thermostable direct hemolysin (TDH). Following results were obtained.
(1) TDH bound to erythrocytes both of which sensitive and insensitive to TDH in similar affinity. Binding of TDH to erythrocytes depends on temperature.
(2) TDH induced phosphorylation of 25 kDa protein on TDH-sensitive erythrocyte membrane but not on TDH-insensitive erythrocyte membrane.
(3) Phosphorylation of 25 kDa protein was inhibited by protein kinase C inhibitors. Hemolytic activity of TDH was also inhibited by protein kinase C inhibitors.
(4) Mutant TDH,R7 which could bind to erythrocytes but lost hemolytic activity, could not induce phosphorylation of 25 kDa protein.
These results suggest that the phosphorylation of 25 kDa protein on erythrocyte membrane is essential to lead erythrocytes lysis.
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