| Project/Area Number |
07670320
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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 | University of Shizuoka |
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Principal Investigator |
YANAGIHA Yasutake University of Shizuoka, School of Pharmaceutical Sciences, Department of Microbiology, Professor, 薬学部, 教授 (30046255)
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| Co-Investigator(Kenkyū-buntansha) |
MASUZAWA Toshiyuki University of Shizuoka, School of Pharmaceutical Sciences, Department of Microbi, 薬学部, 助手 (10181645)
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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 |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1996: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1995: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Lyme disease / Borrelia / Borrelia burgdorferi / Outer surface protein / Adhesion molecule / Virulence factor / Ganglioside / Transcriptional regulation / Borrelia / OspC / OspA / OspB / 接着因子 / 糖脂質 / ガラクトシルセラミド |
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| Research Abstract |
A binding activity of Borrelia burgdorferi, Lyme disease Borrelia, to glycosphingolipids which present in various types of cells was examined. B.burgdorferi bound specifically to galactosylceramide (GalCer) and glucosylceramide, but not to other glycosphingolipids determined by thin layr chromatography (TLC) overlay assay. The binding specificity of B.burgdorferi to various glycosphingolipids suggested that the binding receptor of B.burgdorferi is ceramide monohexoside. Virulent low-passaged strains of B.burgdorferi were serially subcultured in BSK II medium and high-passage strains did not have infectivity to mice or induce footpad swelling. The binding activity of the low-passage strains to GalCer on TLC plate and to CHO-Kl cells in vitro was higher than that of high-passage strains and the binding was not affected by pretreatment of Borrelia with monospecific-anti OspC serum. The results indicated that the binding of Borrelia to the glycosphingolipid being expressed on cell surface play an essential role in the infection to mammalian host. However, OspC do not associate with the binding. It is revealed that recognition of the sugar and N-acyl moieties in galactosylceramide by B.burgdorferi is required for the binding of Borrelia in TLC overlay assay using chemically modified GalCer. Furthermore, three proteins, 67kDa protein, 62kDa Hsp60 and 41kDa flagellin of B.burgdorferi were involved in binding to galactosylceramide as shown by blotting assay probed with biotinylGalCer.
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