| Project/Area Number |
12670246
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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 | Graduate School of Agricultural Science, Tohoku University |
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Principal Investigator |
TOMITA Toshio Graduate School of Agricultural Science, Tohoku University, Associate Professor, 大学院・農学研究科, 助教授 (00126129)
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIYUKI Kamio Graduate School of Agricultural Science, Tohoku University, Professor, 大学院・農学研究科, 教授 (00109175)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2001: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2000: ¥2,500,000 (Direct Cost: ¥2,500,000)
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| Keywords | Staphylococcus aureus / bi-component cytolysins / staphylococcal gamma-hemolysin / staphylococcal leukocidin / serum inhibitor / vitornectin / extracellular matrix |
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| Research Abstract |
Staphylococcal γ-hemolysin and leukocidin are bi-component cytolysins, consisting of LukF (or Hlg1)/Hlg2 and LukF/LukS, respectively. We have previously purified a serum inhibitor of γ-hemolysin and leukocidin, and identified it as vitronectin. In this study, we showed that (i) vitronectin fragments specifically bound to the Hlg2 component of γ-hemolysin and the LukS component of leukocidin to prevent the toxin-induced lysis of human erythrocytes and human polymorphonuclear leukocytes, respectively, (ii) vitronectin fragments and Hlg2 component (or LukS component) formed high-molecular-weight complexes that co-sedimented in a sucrose gradient centrifugation and co-migrated on a native polyacrylamide gel electrophoresis, (iii) the co-sedimented complexes contained vitronectin and the toxin component in an approximate molar ratio of 6 : 1, and (iv) the complexes had spherical shape with diameter of approximately 20 nm. The ability of γ-hemolysin and leukocidin to bind vitronectin is a novel function of the pore-forming cytolysins.
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