Development of bollworms, Helicoverpa zea, on two commercial Bollgard cultivars that differ in overall Cry1Ac levels

J Insect Sci. 2004:4:32. doi: 10.1093/jis/4.1.32. Epub 2004 Oct 8.

Abstract

Research was conducted to quantify the development of the corn earworm (= bollworm), Helicoverpa zea (Boddie), on two different transgenic cotton cultivars (DP 50B and NuCOTN 33B) that contained different levels of the Cry1Ac endotoxin from the soil bacterium, Bacillus thuringiensis Berliner. Using a field cage, an inverse relationship between the amount of Cry1Ac among cultivars versus the weight of bollworm larvae was observed. Larvae that were recovered from the DP 50B cultivar expressing lower Cry1Ac weighed significantly more than larvae collected from the higher expressing NuCOTN 33B cultivar. Cotton plants from NuCOTN 33B were measured as expressing 300% more Cry1Ac than DP 50B plants. The distribution of larval weights indicates that more late-instars (> 200 mg) were collected from the lower expressing DP50B cultivar than the higher expressing NuCOTN 33B cultivar. Within a single population, bollworm larvae were highly variable in their development when feeding on Bollgard cotton. Possible reasons and consequences for this variation are discussed.

MeSH terms

  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism*
  • Body Weight
  • Dose-Response Relationship, Drug
  • Endotoxins / genetics
  • Endotoxins / metabolism*
  • Gene Expression Regulation, Plant
  • Gossypium / genetics
  • Gossypium / metabolism
  • Gossypium / parasitology*
  • Hemolysin Proteins
  • Larva / drug effects
  • Larva / growth & development
  • Moths / drug effects
  • Moths / growth & development*
  • Plants, Genetically Modified / metabolism
  • Plants, Genetically Modified / parasitology

Substances

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