Abstract
Cry toxins from Bacillus thuringiensis are used for insect control. Their primary action is to lyse midgut epithelial cells. In this review we will summarize recent findings on the Cry toxin-receptor interaction and the role of receptor recognition in their mode of action. Cry toxins interact sequentially with multiple receptors. In lepidopteran insects, Cry1A monomeric toxins interact with the first receptor and this interaction triggers oligomerization of the toxins. The oligomer then interacts with second receptor inducing insertion into membrane microdomains and larval death. In the case of mosquitocidal toxins, Cry and Cyt toxins play a part. These toxins have a synergistic effect and Cyt1Aa overcomes Cry toxin resistance. Recently, it was proposed that Cyt1Aa synergizes or suppresses resistance to Cry toxins by functioning as a membrane-bound receptor for Cry toxin.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Review
MeSH terms
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Bacillus thuringiensis / metabolism*
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Bacillus thuringiensis Toxins
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Bacterial Proteins / pharmacology
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Bacterial Toxins / chemistry
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Bacterial Toxins / metabolism*
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Bacterial Toxins / pharmacology
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Dimerization
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Endotoxins / chemistry
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Endotoxins / metabolism*
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Endotoxins / pharmacology
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Hemolysin Proteins / chemistry
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Hemolysin Proteins / metabolism*
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Hemolysin Proteins / pharmacology
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Insect Proteins / metabolism*
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Protein Binding
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Receptors, Cell Surface / metabolism*
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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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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Receptors, Cell Surface
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insecticidal crystal protein, Bacillus Thuringiensis