1995 Fiscal Year Final Research Report Summary
Ultrastructural Analysis of Pore-Formation by Streptolysin 0
| Project/Area Number |
06670303
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | Kitasato University |
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Principal Investigator |
SEKIYA Kachiko Kitasato Univ., Sch.of Pharm.Sci., Lecture, 薬学部, 講師 (30050579)
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| Co-Investigator(Kenkyū-buntansha) |
DANBARA Hirofumi Kitasato Univ., Sch.of Pharm.Sci., Prof., 薬学部, 教授 (40114558)
FUTAESAKU Yutaka Kitasato Univ., Sch.of Allied Health Sci., Prof., 医療衛生学部, 教授 (50014197)
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| Project Period (FY) |
1994 – 1995
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| Keywords | Streptolysin 0 / SLO / Hemolysis / Negative staining / Lyposome / Immuno-electron microscopy / Pore-forming toxin / Electron energy loss spectroscopy |
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| Research Abstract |
The mechanism of pore formation by streptolysin 0 (SLO) on the erythrocyte membrane was ultrastrucurally analyzed by the methods of negatively stained, immuno-electron microscopy, and electron spectroscopic imaging.
When SLO was applied to the erythrocyte membrane at 0ﾟC for 3 to 10 min, no ring-shaped structure was detected. But in the case of the specimen was then treated with anti-SLO and colloidal gold-conjugated anti-IgG for each 20 min at room temperature, the gold particles bound to the membrane were observed. These result indicated that the first step, the binding of SLO molecules to the erythrocyte-membrane was temperature independent.
A hole with SLO-ring was found on the membrane after rising the incuvation temperature up to 37ﾟC for 3 min. This result suggests that the second step that the molecules meet together, and form the rings with holes was temperature dependent.
Furthermore, it was confirmed that the ring structure forming on the liposome by SLO also composed of a double layr of an inner and an outer with a crown.
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