Brush border membrane binding properties of Bacillus thuringiensis Vip3A toxin to Heliothis virescens and Helicoverpa zea midguts
Autor: | Paul J. Miles, Jeng-Shong Chen, Mi Kyong Lee |
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Rok vydání: | 2006 |
Předmět: |
Brush border
Bacterial Toxins Biophysics Receptors Cell Surface medicine.disease_cause Biochemistry Bacterial Proteins Bacillus thuringiensis Botany medicine Animals Intestinal Mucosa Receptor Molecular Biology Cells Cultured Binding Sites Microvilli biology Heliothis virescens Chemistry Toxin Vesicle fungi Cell Biology biology.organism_classification Lepidoptera Cry1Ac Insect Proteins Helicoverpa zea Protein Binding |
Zdroj: | Biochemical and Biophysical Research Communications. 339:1043-1047 |
ISSN: | 0006-291X |
Popis: | The binding properties of Vip3A, a new family of Bacillus thuringiensis insecticidal toxins, have been examined in the major cotton pests, Heliothis virescens and Helicoverpa zea. Vip3A bound specifically to brush border membrane vesicles (BBMV) prepared from both insect larval midguts. In order to examine the cross-resistance potential of Vip3A to the commercially available Cry1Ac and Cry2Ab2 toxins, the membrane binding site relationship among these toxins was investigated. Competition binding assays demonstrated that Vip3A does not inhibit the binding of either Cry1Ac or Cry2Ab2 and vice versa. BBMV protein blotting experiments showed that Vip3A does not bind to the known Cry1Ac receptors. These distinct binding properties and the unique protein sequence of Vip3A support its use as a novel insecticidal agent. This study indicates a very low cross-resistance potential between Vip3A and currently deployed Cry toxins and hence supports its use in an effective resistance management strategy in cotton. |
Databáze: | OpenAIRE |
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