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The crystal proteins from Bacillus thuringiensis subsp. thompsoni display a synergistic activity against the codling moth, Cydia pomonella

Rang Cécile, Lacey Lawrence A., Frutos Roger. 2000. The crystal proteins from Bacillus thuringiensis subsp. thompsoni display a synergistic activity against the codling moth, Cydia pomonella. Current Microbiology, 40 : 200-204.

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Résumé : Crystal proteins from Bacillus thuringiensis subsp. thompsoni strain HnC are active against the codling moth, Cydia pomonella, a major pest of orchards. Inclusion bodies purified from strain HnC displayed an LC50 of 3.34 X 10-3 pg/p1. HnC-purified crystals were tenfold more active than Cry2Aa and Cry1Aa toxins, and 100-fold more toxic than Cry1Ab. The 34-kDa and 40-kDa proteins contained in HnC inclusion bodies were shown to act synergistically. The toxicity of crystal proteins produced by the recombinant B. thuringiensis strain BT-OP expressing the full-length native operon was about tenfold higher than that of the 34-kDa protein. When the gene encoding the non-insecticidal 40-kDa protein, which is not active, was introduced into the recombinant strain producing only the 34-kDa protein, the toxicity was raised tenfold and was similar to that of the strain BT-OP.

Mots-clés Agrovoc : protéine microbienne, Bacillus thuringiensis, lutte anti-insecte, pesticide bactérien, Cydia pomonella

Classification Agris : H10 - Ravageurs des plantes

Auteurs et affiliations

  • Rang Cécile, CIRAD-AMIS-BIOTROP (FRA)
  • Lacey Lawrence A., USDA (USA)
  • Frutos Roger, CIRAD-AMIS-PROTECTION DES CULTURES (FRA)

Autres liens de la publication

Source : Cirad - Agritrop (https://agritrop.cirad.fr/475647/)

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