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

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.

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Bibliographic Details
Main Authors: Rang, Cécile, Lacey, Lawrence A., Frutos, Roger
Format: article biblioteca
Language:eng
Subjects:H10 - Ravageurs des plantes, protéine microbienne, Bacillus thuringiensis, lutte anti-insecte, pesticide bactérien, Cydia pomonella, http://aims.fao.org/aos/agrovoc/c_12537, http://aims.fao.org/aos/agrovoc/c_761, http://aims.fao.org/aos/agrovoc/c_3885, http://aims.fao.org/aos/agrovoc/c_767, http://aims.fao.org/aos/agrovoc/c_30368,
Online Access:http://agritrop.cirad.fr/475647/
http://agritrop.cirad.fr/475647/1/475647.pdf
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Summary: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.