Abstract
The Cry1Ac toxin from Bacillus thuringiensis was displayed on the surface of T7 phage. The cry1Ac gene was fused to the C-terminal end of T7-10B capsid protein and displayed on the surface of T7 phage as revealed by Western blot analysis of the purified phage particles. The T7-Cry1Ac phages retained toxicity against Manduca sexta larvae. We demonstrated that the T7-Cry1Ac phage interacts with Cry1Ac receptors present in M. sexta BBMV either in solution or in overlay binding assays.
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.
MeSH terms
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Animals
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Bacillus thuringiensis / physiology*
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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 Toxins / chemistry
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Bacterial Toxins / genetics
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Bacterial Toxins / metabolism*
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Bacteriophage T7 / genetics*
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Blotting, Western
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Cloning, Molecular
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Electrophoresis, Polyacrylamide Gel
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Genetic Vectors
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Larva
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Manduca / metabolism
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Pest Control, Biological / methods*
Substances
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Bacterial Proteins
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Bacterial Toxins