STRUCTURE AND FUNCTION OF RECEPTOR FOR CLOSTRIDIUM BOTULINUM TYPE B NEUROTOXIN
| Project/Area Number |
06660408
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied veterinary science
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| Research Institution | Osaka Prefecture University |
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Principal Investigator |
KOZAKI Shunji Osaka Prefecture University, Department of Agriculture, Associate Professor., 農学部, 助教授 (10109895)
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| Co-Investigator(Kenkyū-buntansha) |
KAMATA Yoichi Osaka Prefecture University, Department of Agriculture, Research Associate., 農学部, 助手 (20152837)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | Clostridium botulinum / neurotoxin / receptor |
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| Research Abstract |
Clostridium botulinum neurotoxin acts on nerve ending to inhibit neurotransmitter release. The toxin consists of heavy and light chains. The toxic action involves the binding to a type-specific receptor via the heavy chain, endocytosis, and translocation of the light chain into cytosol. We have identified the 58-kDa protein from rat brain synaptosomes, to which type B neurotoxin (BoNT/B) binds only in the presence of gangliosides GT1b/GD1a. Partial amino acid sequence revealed that the 58-kDa protein was identical to those of synaptotagmin, an integral membrane protein of synaptic vesicles. This results were also confirmed that BoNT/B bound specifically to recombinant rat synaptotagmins I and II.Scatchard plot analysis showed a single class of binding site with dissociation constants of 0.23 and 2.3 nM for synaptotagmin II and synaptotagmin I,respectively. The high-affinity binding of BoNT/B was specifically inhibited by a monoclonal antibody recognizing with the amino-terminal region of synaptotagmin II.Although the precise structure of the complex of synaptotagmin and gangliosides remains to be established, these findings indicate that synaptotagmin is a potential candidate acting as BoNT/B protein receptor.
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Report
(3 results)
Research Products
(11 results)
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[Publications] Nishiki, T,Kamata, Y., Nemoto, Y., Omori, A., Ito, T., Takahashi, M., and Kozaki, S.: "Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes." Journal of Biological Chemistry. 269. 10498-10503 (1994)
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[Publications] Nishiki, T., Tokuyama, Y., Kamata, Y.Nemoto, Y., Yoshida, A., Sato, K., Sekiguchi, M., Takahashi, M., and Kozaki, S: "The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with ganglioside GT1b" FEBS Lett. 378. 253-257 (1996)
Description
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