Oligomerization of Cry11Aa from Bacillus thuringiensis has an important role in toxicity against Aedes aegypti

Appl Environ Microbiol. 2009 Dec;75(23):7548-50. doi: 10.1128/AEM.01303-09. Epub 2009 Oct 9.

Abstract

Cry11Aa and Cyt1Aa of Bacillus thuringiensis are active against mosquitoes and show synergism. Cyt1Aa functions as a membrane receptor inducing Cry11Aa oligomerization. Here we characterized Cry11Aa helix alpha-3 mutants impaired in oligomerization and toxicity against Aedes aegypti, indicating that oligomerization of Cry11Aa is important for toxin action. Cyt1Aa did not recover the insecticidal activity of Cry11Aa mutants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aedes / drug effects*
  • Animals
  • Bacillus thuringiensis / metabolism*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / toxicity*
  • Endotoxins / genetics
  • Endotoxins / metabolism*
  • Endotoxins / toxicity*
  • Hemolysin Proteins / genetics
  • Hemolysin Proteins / metabolism*
  • Hemolysin Proteins / toxicity*
  • Protein Multimerization
  • Sequence Deletion

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis