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Creation of proteinaceous insecticide from Bacuillus thuringlensis δ-endotoxin and single chain variable fragment

Research Project

Project/Area Number 09558076
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section展開研究
Research Field 環境保全
Research InstitutionTokyo University of Agriculture & Technology

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)

Co-Investigator(Kenkyū-buntansha) IWAHATA Hidenori  Tokyo University of Agriculture and Technology, Faculty of Agriculture, Professor, 農学部, 教授 (90038240)
Project Period (FY) 1997 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥8,900,000 (Direct Cost: ¥8,900,000)
Fiscal Year 1999: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1998: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 1997: ¥5,200,000 (Direct Cost: ¥5,200,000)
KeywordsBacillus thuringiensis / δ-endotoxin / single chain variable / insecticide / アミノペプチターゼN / δ内毒素 / 殺虫剤
Research Abstract

Creation of proteinaceous insecticide was challenged using Bacillus thuringiensis δ-endotoxin and single chain variable fragment of monoclonal antibody as materials.
Monoclonal antibody was constructed against membrane protein of the midgust from longicorn beetle. Acalolepta luxuriosa and single chain variable fragment was made from the antibody. single chain variable fragment and Bacillus thuringiensis δ-endotoxin was connected by geen engineering and binding capability of the chimera-proteins were confirmed. From now on we will assess the insecticidal activity of the proteins using Acalolepte luxuriosa.
On the other hand, receptor of the Cry1Aa δ-endotoxin on the midgut of the silkworm, Bombyx mori was researched to know indispensable nature for the activity of the target molecule of the δ-endotoxin since it seems most important for the activity of the chimera-protein to select appropriate molecules as targets of the single chain variable. As a result, it was shown that Cry1Aa and Cry9Da utilize aminopeptidase N as a receptor on the midgut cells of the silkworm. Cry1Aa bound to N terminal region of aminopeptidase N consisting of about 60 amino acid residues.

Report

(4 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • 1997 Annual Research Report
  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] K. Yaoi: "cDNA cloning and expression of Bacillus thuringiensis Cry1Aa toxin binding 120 kDa aminopeptidase N from Bombyx mori"Biochim biophys Acta. 1444. 131-137 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] A. Shinkawa: "Binding of phylogenetically distant Bacillus thuringiensis Cry toxins to a Bombyx mori aminopeptidase N suggests importance of Cry toxin's conserved structure in"Current Microbiol.. 39. 14-20 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] N. K. Yaoi: "Bacillus thringiensis Cry 1Aa toxin binding region of bombyx mori aminopeptidase"FEBS Lett.. 463. 221-224 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] K. Nakanishi: "Bacillus thuringiensis insecticedal protein Cry 1Aa binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary success"Biochim Biophys Acta. 1432. 57-63 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] K. Yaoi et al.: "cDNA cloning and expression of Bacillus thuringienses CrylAa toxin binding 120 kDa aminopepetidase N from Bombyx mori"Biochim Biophys Acts. 1444. 131-137 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] A. Shinkawa et al.: "Binding of phylogenetically distant Bacillus thuringienses Cry toxins to a Bombyx mori aminopeptidase N suggests importance of Cry toxin's conserved structure in receoptor binding"Current Microbiol.. 39. 14-20 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] N. K. Yaoi et al.: "Bacillus thuringienses Cry 1Aa toxin binding region of Bombyx mori aminopeptidase"FEBS Lett.. 463. 221-224 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] K. nakanishi et al.: "Bacillus thuringienses inspecticedal protein Cry 1Aa binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary success"Biochim Biophys Acta. 1432. 57-63 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] K.Yaoi: "cDNA cloning and expression of Bacillus thuringiensis Cry 1Aa toxin binding 120 kDa aminopeptidase N from Bombyx mori."Biochim Biophys Acta. 1444. 131-137 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] A.Shinkawa: "Binding of phylogenetically distant Bacillus thuringiensis Cry toxins to a Bombyx mori aminopeptidase N suggests importance of Cry toxin's"Current Microbiol.. 39. 14-20 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] N.K.Yaoi: "Bacillus thringiensis Cry 1Aa toxin binding region of Bombyx mori aminopeptidase."FEBS Lett.. 463. 221-224 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] K.Nakanishi: "Bacillus thuringiensis insecticedal protein Cry 1Aa binds to a highly conserved region of aminopeptidase N in the host insect leading to its evolutionary"Biochim Biophys Acta. 1432. 57-63 (1999)

    • Related Report
      1999 Annual Research Report

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

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