1999 Fiscal Year Final Research Report Summary
Quantitative Analysis of Receptor Function of Ganglioside Lactone
| Project/Area Number |
09680584
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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 |
Structural biochemistry
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| Research Institution | Tokyo Institute of Technology |
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Principal Investigator |
SATO Toshinori Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Associate Professor, 生命理工学部, 助教授 (00162454)
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| Co-Investigator(Kenkyū-buntansha) |
MORI Toshiaki Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Assistant Professor, 生命理工学部, 助手 (50262308)
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| Project Period (FY) |
1997 – 1999
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| Keywords | Ganglioside / Ganglioside Lactone / Monolayer / Saccharide Recognition / Lectin / influenza Virus / Receptor |
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| Research Abstract |
Gangliosides ate known as an antigen on animal cells, a receptor for influenza virus, and a cell adhesion molecule. When subjected to mild acidic condition, gangliosides form an internal ester, so called "lactone", between a carboxyl group of sialic acid and a hydroxyl group of neighboring saccharide. Ganglioside lactones have been detected in tumor cells and normal brain. An IgM monoclonal antibody established after immunization with B16 melanoma showed stronger affinity with GM3 lactone than with GM3. Therefore, ganglioside lactone is considered to be real immunogen on B16 melanoma cells.
In our study, GM3 lactone showed higher binding affinity with a sialic acid-binding protein (wheat germ agglutinin, WGA) than the parent GM3 did. Next, we found that GM3 lactone and GM4 lactone has a potential to bind to influenza virus hemagglutinin without being hydrolyzed by neuraminidase. Influenza virus is known to have membrane proteins such as hemagglutinin and neuraminidase. Hemagglutinin selectively binds to sialylgalactose groups conjugated with lipids. Such the sialylglycolipids are also substrates for neuraminidase. Exploration of glycolipids that are not hydrolyzed by neuraminidase should be important to know the mechanisms for the transfection of influenza virus to host cells, and to develop inhibitors for influenza virus.
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