Back to Search
Start Over
Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella).
- Source :
-
Insect biochemistry and molecular biology [Insect Biochem Mol Biol] 2003 Sep; Vol. 33 (9), pp. 929-35. - Publication Year :
- 2003
-
Abstract
- Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with (125)I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1Ac, and Cry1Ja bound to a common binding site that was not shared by the other toxins tested. Reciprocal competition experiments with Cry1Ab, Cry1Ac, and Cry1Ja showed that these toxins do not bind to any additional binding sites. In the resistant strain, binding of (125)I-Cry1Ac was not significantly affected; however, (125)I-Cry1Ab did not bind to the BBMV. This result, along with previous data from this strain, shows that the resistance fits the "mode 1" pattern of resistance described previously in Plutella xylostella, Plodia interpunctella, and Heliothis virescens.
- Subjects :
- Animals
Bacillus thuringiensis genetics
Bacterial Toxins genetics
Binding Sites
Binding, Competitive
Cytoplasmic Vesicles metabolism
Iodine Radioisotopes
Kinetics
Larva microbiology
Lepidoptera genetics
Microvilli metabolism
Pest Control, Biological
Protein Binding
Radioligand Assay
Recombinant Proteins genetics
Recombinant Proteins metabolism
Bacillus thuringiensis metabolism
Bacterial Toxins metabolism
Lepidoptera metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0965-1748
- Volume :
- 33
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Insect biochemistry and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 12915184
- Full Text :
- https://doi.org/10.1016/s0965-1748(03)00099-7