| Project/Area Number |
17510179
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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 |
Living organism molecular science
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| Research Institution | Kagoshima University |
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Principal Investigator |
SUDA Yasuo Graduate School of Science and Technology, Kagoshima University, Professor, 理工学研究科, 教授 (70179282)
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| Co-Investigator(Kenkyū-buntansha) |
HASHIMOTO Masahito Kagoshima University, Graduate School of Science and Technology, Associate Professor, 大学院理工学研究科, 助教授 (30333537)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2006: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2005: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Gram-positive bacteria / innate immunity / lipoteichoic acid / lipoprotein / lipopeptide / lipoarabinomannan / separation and purification / neutralizing antibody |
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| Research Abstract |
Many glycoconjugates are located on cell surface of bacteria and shown to activate innate immune system. Lipoteichoic acid (LTA) is a predominant glycoconjugate in Gram-positive bacteria and reported to possessed immunobiological activities. We previously reported that a purified LTA obtained from Enterococcus hirae had no immunostimulatingactivity.butasubfractionintheLTAfraction exerted the activity. In this study, we intended to elucidate a structure and function of the compound responsible for the activity.
We established an antibody neutralizing the activity of the active compound. The antibody neutralized not only LTA fraction from E. hirae but also that from.Staphylococcus aureus. The antibody also inhibited the activity of immunostimulating synthetic lipopeptides. By immunoblotting assay, it is found that the antibody recognized lipopeptides but not their non-lipidated counterparts. These results suggest that lipoprotein-like compounds are responsible for the activity of the LTA fraction.
Lipoi3rabinomannan (LAM) is a major high molecular weight glycoconjugates in acid-fast bacilli and is also reported to cause immune activation. The principal structure for the activity, however, has not been described. In this study, we aimed to elucidate the structure.
The LAM was extracted from Mycobacterium smegmatis and subjected to further purification. A highly active compounds were found in a high-anionic fraction and the activity was abrogated by protease digestion. These results indicated that the proteinous materials are active components in LAM fraction.
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