Abstract
A novel cry1A was cloned from Bacillus thuringiensis strain BT8 and expressed in the B. thuringiensis acrystalliferous mutant HD73(-). The gene, designated cry1Ah1, encoded a protein with a molecular weight of 134 kDa. Reverse transcriptase-PCR and Western blotting showed that Cry1Ah was expressed in the host strain BT8. The toxin expressed in HD73(-) exhibited high toxicity against lepidopteran larvae of Ostrinia furnacalis, Helicoverpa armigera, Chilo suppressalis, and Plutella xylostella. The 50% lethal concentrations (LC(50)s) were 0.05, 1.48, 0.98 microg g(-1) and 1.52 microg mL(-1), respectively. The LC(50)s of Cry1Ah were significantly lower than that of Cry1Ac for H. armigera, C. suppressalis, and O. furnacalis, and lower than that of Cry1Ab and Cry1Ie for Ostrinia furnacalis. The high toxicity against a range of pest species makes this novel toxin a potential candidate for insect biocontrol.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Bacillus thuringiensis / metabolism
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Bacillus thuringiensis / pathogenicity*
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Bacillus thuringiensis / ultrastructure
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Bacillus thuringiensis Toxins
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Bacterial Proteins / toxicity
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Bacterial Toxins / chemistry*
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Bacterial Toxins / genetics*
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Bacterial Toxins / metabolism
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Bacterial Toxins / toxicity
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Cloning, Molecular*
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Endotoxins / chemistry*
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Endotoxins / genetics*
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Endotoxins / metabolism
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Endotoxins / toxicity
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Genes, Bacterial
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Hemolysin Proteins / chemistry*
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Hemolysin Proteins / genetics*
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Hemolysin Proteins / metabolism
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Hemolysin Proteins / toxicity
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Lethal Dose 50
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Microscopy, Electron, Scanning
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Moths / drug effects*
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Pest Control, Biological
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Reverse Transcriptase Polymerase Chain Reaction
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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Endotoxins
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Hemolysin Proteins
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insecticidal crystal protein, Bacillus Thuringiensis