| Project/Area Number |
04670278
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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 |
Virology
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| Research Institution | Jichi Medical School |
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Principal Investigator |
TASHIRO Masato Jichi Medical School, Dept.Virol., Assoc.Prof., 医学部, 助教授 (90111343)
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| Co-Investigator(Kenkyū-buntansha) |
ODAGIRI Takato Jichi Medical School, Dept.Virol., Assis.Prof., 医学部, 講師 (80177237)
TANAKA Toshinori Jichi Medical School, Dept.Virol., Assis.Prof., 医学部, 講師 (30146154)
田代 真人 自治医科大学, 医学部, 助教授 (90111343)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1992: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Sendai virus / Tropism / Tryptase Clara / Budding polarity / Mictotubules / M protein / Epithelial cells / Protein transport / HVJ / F1-R株 / 細胞骨格系 / 細胞内蛋白輸送 / 糖蛋白 / MDCK細胞 |
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| Research Abstract |
1. We isolated and characterized a novel serine-protease designated "Tryptase Clara", present in and secreted from the Clara cells of rat bronchial epithelia. Tryptase Clara was revealed to activate Sendai virus progeny by proteolytic cleavage of the F protein in rat lungs, and thereby facilitate multiple cycles of viral replication and pneumopathology.
2. Budding polarity of Sendai virus at the bronchial epithelial cells, the primary target of infection, was shown to determine the organ tropism. Apical budding by wild-type virus is responsible for licalized infection in the airways, whereas basolateral budding is required for systemic spread of progeny virus to distant organs resulting in a systemic infection.
3. In addition to proteolytic activation of the F protein, basolateral expression of viral glycoproteins is a prerequisite for inducing cell fusion.
4. A mutant Sendai virus, F1-R, which buds bipolarly in epithelial cells, was shown to disrupt microtubule network in infected cells, resulting in impaired cellular polarity. By comparative analysis of the entire nucleotide sequence of wild-type and F1-R viruses, the mutated M protein was suggested to be responsible for this phenomenon.
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