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Molecular mechanisms of receptor recognition by Clostridium botulinum neurotoxins.

Research Project

Project/Area Number 09660343
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied veterinary science
Research InstitutionOsaka Prefecture University

Principal Investigator

KOZAKI Shunji  Osaka Prefecture University, Department of Agriculture.Associate Professor, 農学部, 助教授 (10109895)

Project Period (FY) 1997 – 1998
Project Status Completed (Fiscal Year 1998)
Budget Amount *help
¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 1998: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1997: ¥2,300,000 (Direct Cost: ¥2,300,000)
KeywordsClostridium botulinum / neurotoxin / recptor / synaptotagmin / synaptobrevin / ganglioside / ボツリヌス毒素 / 神経毒
Research Abstract

Clostridium botulinum type B neurotoxin recognizes a complex of synaptotagmin II and ganglioside GTlb/GD1a as the high-affinity binding site. Recombinant deletion mutant of synaptotagmin II allowed us to demonstrate that the N-terminal domain including the transmembrane region retain the toxin binding activity while the C-terminal domain is not involved in constituting the toxin receptor. The direct binding of GTlb to the deletion mutants revealed that the transmembrane region is required to bind GTlb, suggesting that synaptotagmin II bind to the ceramide portion of ganglioside within the plasma membrane. Monoclonal antibody against GTlb effectively inhibited not only type B neurotoxin but also type A neurotoxin binding to brain synaptosomes. In addition, the monoclonal antibody antagonized the action of both neurotoxins on synaptic transmisstion of rat superior cervival ganglion neurons. They suggest that GTlb functions as a component of the receptor complex.
The neurotoxin of the strain associated with type B infant botulism showed antigenic and biological properties different from that of food-borne botulism-related strain. The neurotoxin derived from infant botulism was found to possess a toxicity 10 times lower than that of the authentic neurotoxin. However, synaptobrevin, an intracellular target protein, was digested to the same extent by both neurotoxins. Therefore, we concluded that such low toxicity of infant botulism-related neurotoxin is attributed to the receptor-recognition site in the molecule.

Report

(3 results)
  • 1998 Annual Research Report   Final Research Report Summary
  • 1997 Annual Research Report
  • Research Products

    (14 results)

All Other

All Publications (14 results)

  • [Publications] Kamata,Y: "Interaction between botulinum neurotoxin type A and ganglioside" Toxicon. 35,8. 1337-1340 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki,S.: "Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins" Microbiol Pathogenesis. 25,1. 91-99 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki,S.: "Characeterization of Clostridiub botulinum type B neurotoxin associated with infant botulism in Japan" Infection and Immunity. 66,10. 4811-4816 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] 小崎 俊司: "ボツリヌス神経毒素の受容体に関する研究" 日本細菌学雑誌. 印刷中. (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki,S.: "Molecular mechanisms of the action of Clostridium botulinum type B neurotoxin. In Secretory system and toxins." Harwood Academic Publishers, 173-184 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kamata, Y.: "Interaction between botulinum neurotoxin type A and ganglioside : Ganglioside inactivates the neurotoxin and quenches its tryptophan flourescence." Toxicon. 35/8. 1337-1340 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki, S.: "Ganglioside GT1b as a complementray Receptor component for Clostridium botulinum neurotoxins." Microbial Pathogenis. 25/1. 91-99 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki, S.: "Characeterization of Clostridium botulinum type B neurotoxin associated with infant botulism in Japan." Infection and Immunity. 66/10. 4811-4816 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki, S.: "Studies on the receptor for Clostridium botulinum neurotoxin (In Japanese)" Nihon Saikingaku Zatsushi. (in press). (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki, S.: Molecular mechanisms of the action of Clostridium botulinum type B neurotoxin. (In Secretory system and toxins). Harwood Academic Publishers, 173-184 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kozaki,s.: "Ganglioside GT1b as a complementary receptor component for clostridium botulinum neurotoxins." Microbiol Pathogenesis. 25:1. 91-99 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Kozaki,S.: "Characterization of Clostridium botulinum type B neurotoxin associated with infant botulism in Japan." Infection and Immunity. 66:10. 4811-4816 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Kozaki,S.: "Molecular mechanisms of the action of clostridium botulinum type B neurotoxin. In secretory system and toxins." Harwood Acacemic Publishers, 173-184 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Kamata,Y.: "Interaction between botulinum neurotoxiu type A・・・" Toxicon. 35・8. 1337-1340 (1997)

    • Related Report
      1997 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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