Treatment of an Aedes aegypti colony with the Cry11Aa toxin for 54 generations results in the development of resistance

Mem Inst Oswaldo Cruz. 2012 Feb;107(1):74-9. doi: 10.1590/s0074-02762012000100010.

Abstract

To study the potential for the emergence of resistance in Aedes aegypti populations, a wild colony was subjected to selective pressure with Cry11Aa, one of four endotoxins that compose the Bacillus thuringiensis serovar israelensis toxin. This bacterium is the base component of the most important biopesticide used in the control of mosquitoes worldwide. After 54 generations of selection, significant resistance levels were observed. At the beginning of the selection experiment, the half lethal concentration was 26.3 ng/mL and had risen to 345.6 ng/mL by generation 54. The highest rate of resistance, 13.1, was detected in the 54th generation. Because digestive proteases play a key role in the processing and activation of B. thuringiensis toxin, we analysed the involvement of insect gut proteases in resistance to the Cry11Aa B. thuringiensis serovar israelensis toxin. The protease activity from larval gut extracts from the Cry11Aa resistant population was lower than that of the B. thuringiensisserovar israelensis susceptible colony. We suggest that differences in protoxin proteolysis could contribute to the resistance of this Ae. aegypti colony.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / pharmacology*
  • Culex / drug effects*
  • Culex / enzymology
  • Culex / genetics
  • Endotoxins / pharmacology*
  • Hemolysin Proteins / pharmacology*
  • Insecticide Resistance / drug effects
  • Insecticide Resistance / genetics*
  • Lethal Dose 50
  • Peptide Hydrolases / genetics*
  • Selection, Genetic / drug effects
  • Selection, Genetic / genetics*

Substances

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