Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage.
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.
Pacheco
Sabino
S
Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos.
Gómez
Isabel
I
Sato
Ryoichi
R
Bravo
Alejandra
A
Soberón
Mario
M
D000818:Animals; D001413:Bacillus thuringiensis / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017123:Bacteriophage T7 / Q000235:genetics*; D015153:Blotting, Western; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D005822:Genetic Vectors; D007814:Larva; D018402:Manduca / Q000378:metabolism; D010572:Pest Control, Biological / Q000379:methods*
D001426:Bacterial Proteins; D001427:Bacterial Toxins