| Project/Area Number |
24590538
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | Chubu University |
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Principal Investigator |
MIYATA Shigeru 中部大学, 応用生物学部, 准教授 (90314913)
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| Co-Investigator(Kenkyū-buntansha) |
MORIYAMA Ryuichi 中部大学, 応用生物学部, 教授 (60191061)
OKABE Akinobu 中国学園大学, 現代生活学部, 教授 (20093677)
NARIYA Hirofumi 香川大学, 医学部, 助教 (30452668)
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| Co-Investigator(Renkei-kenkyūsha) |
YOSHIDA Hiromi 香川大学, 総合生命科学研究センター, 准教授 (10313305)
NAKAKITA Shinichi 香川大学, 総合生命科学研究センター, 准教授 (40314356)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | Clostridium perfringens / hyaluronidase / ウェルシュ菌 / 糖鎖分解酵素 / 発現系 / 病原性 |
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| Outline of Final Research Achievements |
Clostridium perfringens is notable for their genomic content of numerous open-reading frames that encode carbohydrate-active enzymes. Among them, hyaluronidase is thought to function as virulence factors. This enzyme is believed to spread the organism in infected tissues or potentiate other toxins through facilitation of their diffusion via the degradation of hyaluronan, NagH has been partially purified as hyaluronidase from the organism (Canard, et al., 1994).
In this study, we successfully purified NagH and the products of nagH paralogs, NagI, NagJ, NagK and NagL with high quality from recombinant C. perfringens cultures. These recombinant enzymes exhibit exo-N-acetyl-β-glucosaminidase activity but not hyaluronan degrading activity. These results led us question whether C. perfringens Nag(s) could genuinely hydrolyze hyaluronan. Thus, we searched and found a genuine gene of hyaluronidase in the organism, and indicated that the product exhibits hyaluronan degrading activity.
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