| Project/Area Number |
23570068
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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 |
Morphology/Structure
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| Research Institution | Saitama University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
KIKUYAMA Sakae 早稲田大学, 教育・総合学術院, 名誉教授 (20063638)
IWAMURO Shawichi 東邦大学, 理学部, 教授 (70221794)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 抗菌ペプチド / 生体防御 / ファブリキウス嚢 / ハーダー腺 / fowlicidin |
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| Research Abstract |
We intended to obtain cDNAs encoding precursor for antimicrobial peptide fowlicidin (f)-1, -2, and -3 from total RNA samples prepared from the quail bursa of Fabricius (BF) and Harderian gland (HG) by RT-PCR. As a result, f-1, -2, and -3 cDNAs were invariably obtained from the BF. However, only f-2 cDNA was detected in HG, so far studied. In situ hybridization and immunocytohistochemical analyses revealed that f-2 is expressed in the epithelium of lumen and the lymphoid follicles in the BF. Synthetic f-2 exerted a growth-inhibiting activity toward the gram-negative bacterium Escherichia coli and gram-positive bacterium Staphylococcus aureus through the destructing the bacterial membrane. Lipopolysaccharide (LPS)-binding assay showed that f-2 possessed an ability to bind the bacterial LPS, which is a constituent of the outer membrane of the gram-negative bacteria. The endotoxin-neutralizing activity of f-2 was also confirmed by the Lymulus amebocyte lysate assay.
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