Efficacy of Bacillus thuringiensis Cry3Aa protoxin and protease inhibitors against coleopteran storage pests

Pest Manag Sci. 2011 May;67(5):568-73. doi: 10.1002/ps.2099. Epub 2011 Jan 26.

Abstract

Background: Environmental impacts and resistance to insecticides pose serious challenges to stored-product insect and other types of pest control. Insect-resistant transgenic grain is a potential alternative to fumigants, but candidate control proteins are needed, especially for coleopterans. Therefore, we evaluated the efficacy of a coleopteran-active toxin, Bacillus thuringiensis Cry3Aa, with or without protease inhibitors, in laboratory feeding assays against coleopteran storage pests.

Results: In a comparison of the toxicity of Cry3Aa protoxin towards three species of coleopteran storage pests, Tenebrio molitor L. was found to be most sensitive, Tribolium castaneum (Herbst.) was most refractory and Rhyzopertha dominica F. displayed an intermediate response. For R. dominica, Cry3Aa combined with 3500 mg potato carboxypeptidase inhibitor or 5000 mg aprotinin kg(-1) diet resulted in both delayed development and increased mortality. Potato carboxypeptidase inhibitor and bovine aprotinin reduced the LC(50) of Cry3Aa for R. dominica two- and threefold respectively. Cry3Aa treatment resulted in fewer progeny from R. dominica, and progeny was further reduced when the protoxin was combined with potato carboxypeptidase inhibitor.

Conclusions: These data support the hypothesis that a combination of Cry3Aa protoxin and protease inhibitors, particularly a potato carboxypeptidase inhibitor, may have applications in control strategies for preventing damage to stored products and grains by coleopteran pests.

MeSH terms

  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / pharmacology*
  • Coleoptera / drug effects*
  • Coleoptera / growth & development
  • Endotoxins / pharmacology*
  • Hemolysin Proteins / pharmacology*
  • Insecticides / pharmacology*
  • Pest Control, Biological / methods*
  • Protease Inhibitors / pharmacology*

Substances

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