Analysis of Cry8Ka5-binding proteins from Anthonomus grandis (Coleoptera: Curculionidae) midgut

J Invertebr Pathol. 2010 Jul;104(3):227-30. doi: 10.1016/j.jip.2010.01.012. Epub 2010 Feb 6.

Abstract

Biotech crops expressing Bacillus thuringiensis Cry toxins present a valuable approach for insect control. Cry8Ka5, which is highly toxic to the cotton boll weevil (Anthonomus grandis), was used as a model to study toxin-ligand interactions. Three Cry-binding proteins were detected after toxin overlay assays. Following de novo sequencing, a heat-shock cognate protein and a V-ATPase were identified, whilst a approximately 120 kDa protein remained unknown. Additional Cry8Ka5-binding proteins were visualized by two-dimensional gel electrophoresis ligand blots.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis / metabolism*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Digestive System / metabolism*
  • Endotoxins / chemistry
  • Endotoxins / metabolism*
  • HSC70 Heat-Shock Proteins / analysis
  • HSC70 Heat-Shock Proteins / metabolism
  • Hemolysin Proteins / chemistry
  • Hemolysin Proteins / metabolism*
  • Insecticides / chemistry
  • Insecticides / metabolism*
  • Larva / metabolism
  • Pest Control, Biological / methods*
  • Protein Binding
  • Vacuolar Proton-Translocating ATPases / analysis
  • Vacuolar Proton-Translocating ATPases / metabolism
  • Weevils / metabolism*

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • HSC70 Heat-Shock Proteins
  • Hemolysin Proteins
  • Insecticides
  • insecticidal crystal protein, Bacillus Thuringiensis
  • Vacuolar Proton-Translocating ATPases