Research for a basic anti-microbial recognition system of the animal using silkworm, Bombyx mori
| Project/Area Number |
10680601
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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 |
Functional biochemistry
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| Research Institution | Tokyo University of Agriculture & Technology |
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Principal Investigator |
SATO Ryoichi Tokyo University of Agriculture and Technology, Graduate School of Bio-Applications and Systems-engineering, Associate Professor, 大学院・生物システム応用科学研究科, 助教授 (30235428)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1999: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1998: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | C-type lectin / BmLBP / Bombyx mori / recognition protein / Bombyx mori |
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| Research Abstract |
Affinity purification was conducted with microbial cells to obtain anti-microbial recognition proteins from the larval hemolymph of the silkworm. Bombyx mori.
A 43 kDa lipopolysaccharide-binding protein was purified with Esherichia coli cells and named BmLBP. BmLBP bound to many kinds of gram-negative bacteria by recognition of lipid A and helped nodule formation of the blood cells. From the result of cDNA cloning and sequencing it was shown that BmLBP is a novel member of the C-type lectin superfamily with a unique structural feature that consists of two different carbohydrate-recognition domains in tandem.
Two proteins of 42 kDa were purified respectively with Saccharomyces cervisiae cells and Micrococcus luteus cells. Both bound bacteria by recognizing carbohydrate of the bacterial cell wall. Also, they needed calcium in binding. From these characters two protein were assumed to be C-type lectins.
Antisera were constructed against these three binding proteins and closs-reactivity was tested each other. As a result, two protein obtained with Saccharomyces cervisiae cells and Micrococcus luteus cells were shown to be selologically the same and BmLBP was shown to be different from these two proteins. From these results it was supposed that only two kinds of lectin is sufficient to recognize fairly broad range of microorganisms.
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Report
(3 results)
Research Products
(6 results)
