Abstract
Environmentally friendly toxins of Bacillus thuringiensis are effective in controlling agriculturally and biomedically harmful insects. However, little is known about the insect receptor molecules that bind these toxins and the mechanism of insecticidal activity. We report here for the first time the cloning and expression of a cDNA that encodes a receptor (BT-R1) of the tobacco hornworm Manduca sexta for an insecticidal toxin of B. thuringiensis. The receptor is a 210-kDa membrane glycoprotein that specifically binds the cryIA(b) toxin of B. thuringiensis subsp. berliner and leads to death of the hornworm. BT-R1 shares sequence similarity with the cadherin superfamily of proteins.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Bacillus thuringiensis Toxins
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Bacillus thuringiensis*
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Bacterial Proteins / metabolism*
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Bacterial Toxins*
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Binding, Competitive
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Blotting, Northern
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Cadherins / chemistry*
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Cadherins / genetics*
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Cell Line
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Cloning, Molecular
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Consensus Sequence
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Digestive System / metabolism
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Drosophila
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Endotoxins / metabolism*
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Gene Expression
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Hemolysin Proteins
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Humans
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Insect Proteins*
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Kinetics
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Manduca
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Mice
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Pest Control, Biological
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Protein Biosynthesis
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Receptors, Cell Surface / biosynthesis*
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism*
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Sequence Homology, Amino Acid
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Transfection
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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Cadherins
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Cry toxin receptors
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Endotoxins
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Hemolysin Proteins
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Insect Proteins
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Peptide Fragments
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Receptors, Cell Surface
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insecticidal crystal protein, Bacillus Thuringiensis