Functional display of Bacillus thuringiensis Cry1Ac toxin on T7 phage

J Invertebr Pathol. 2006 May;92(1):45-9. doi: 10.1016/j.jip.2006.02.007. Epub 2006 Apr 17.

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

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Bacillus thuringiensis / physiology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism*
  • Bacteriophage T7 / genetics*
  • Blotting, Western
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Genetic Vectors
  • Larva
  • Manduca / metabolism
  • Pest Control, Biological / methods*

Substances

  • Bacterial Proteins
  • Bacterial Toxins