Abstract.
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 × 10−3μg/μl. 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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Received: 25 August 1999 / Accepted: 5 October 1999
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Rang, C., Lacey, L. & Frutos, R. The Crystal Proteins from Bacillus thuringiensis subsp. thompsoni Display a Synergistic Activity Against the Codling Moth, Cydia pomonella . Curr Microbiol 40, 200–204 (2000). https://doi.org/10.1007/s002849910040
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DOI: https://doi.org/10.1007/s002849910040