Broad-spectrum resistance to Bacillus thuringiensis toxins in Heliothis virescens.
- 1 September 1992
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 89 (17) , 7986-7990
- https://doi.org/10.1073/pnas.89.17.7986
Abstract
Evolution of pest resistance to insecticidal proteins produced by Bacillus thuringiensis (Bt) would decrease our ability to control agricultural pests with genetically engineered crops designed to express genes coding for these proteins. Previous genetic and biochemical analyses of insect strains with resistance to Bt toxins indicate that (i) resistance is restricted to single groups of related Bt toxins, (ii) decreased toxin sensitivity is associated with changes in Bt-toxin binding to sites in brush-border membrane vesicles of the larval midgut, and (iii) resistance is inherited as a partially or fully recessive trait. If these three characteristics were common to all resistant insects, specific crop-variety deployment strategies could significantly diminish problems associated with resistance in field populations of pests. We present data on Bt-toxin resistance in Heliothis virescens, a major agricultural pest targeted for control with Bt-toxin-producing crops. A laboratory strain of H. virescens developed resistance in response to selection with the Bt toxin CryIA(c). In contrast to other cases of Bt-toxin resistance, this H. virescens strain exhibits cross-resistance to Bt toxins that differ significantly in structure and activity. Furthermore, the resistance in this strain is not accompanied by significant changes in toxin binding, and resistance is inherited as an additive trait when larvae are treated with high doses of CryIA(c) toxin. These findings have important implications for Bt-toxin-based pest control.Keywords
This publication has 14 references indexed in Scilit:
- Binding of Bacillus thuringiensis proteins to a laboratory-selected line of Heliothis virescens.Proceedings of the National Academy of Sciences, 1991
- The toxicity of twoBacillus thuringiensis δ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxinsCellular and Molecular Life Sciences, 1990
- Mechanism of Insect Resistance to the Microbial Insecticide Bacillus thuringiensisScience, 1990
- Specificity of Bacillus thuringiensisδ‐endotoxinsEuropean Journal of Biochemistry, 1989
- Genetically Engineering Plants for Crop ImprovementScience, 1989
- Insecticidal crystal proteins of Bacillus thuringiensis.1989
- Nucleotide sequence of crystal protein gene isolated from B.thuringiensis subspecies entomocidus 60.5 coding for a toxin highly active against Spodoptera speciesNucleic Acids Research, 1988
- Bacillus sphaericusstrain 2297: nucleotide sequence of 41.9 kDa toxin geneNucleic Acids Research, 1988
- LIGAND: A versatile computerized approach for characterization of ligand-binding systemsAnalytical Biochemistry, 1980
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976