title: Shared binding sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A toxins.
abstract: Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth (Plutella xylostella) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that Cry1Ja shares binding sites with Cry1A toxins. We tested this hypothesis in six moth and butterfly species, each from a different family: Cacyreus marshalli (Lycaenidae), Lobesia botrana (Tortricidae), Manduca sexta (Sphingidae), Pectinophora gossypiella (Gelechiidae), P. xylostella (Plutellidae), and Spodoptera exigua (Noctuidae). Although the extent of competition varied among species, experiments with biotinylated Cry1Ja and radiolabeled Cry1Ac showed that Cry1Ja and Cry1Ac competed for binding sites in all six species. A recent report also indicates shared binding sites for Cry1Ja and Cry1A toxins in Heliothis virescens (Noctuidae). Thus, shared binding sites for Cry1Ja and Cry1A occur in all lepidopteran species tested so far.
authors.affiliation: Department of Genetics, University of Valencia, 46100-Burjassot (Valencia), Spain.
authors.forename: S
authors.initials: S
authors.lastname: Herrero
authors.forename: J
authors.initials: J
authors.lastname: González-Cabrera
authors.forename: B E
authors.initials: BE
authors.lastname: Tabashnik
authors.forename: J
authors.initials: J
authors.lastname: Ferré
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity; D001427:Bacterial Toxins; D001665:Binding Sites; D001667:Binding, Competitive; D004731:Endotoxins / Q000235:genetics / Q000378:metabolism* / Q000633:toxicity; D006460:Hemolysin Proteins; D007305:Insecticide Resistance; D007814:Larva / Q000378:metabolism; D007915:Lepidoptera / Q000187:drug effects / Q000378:metabolism*; D008969:Molecular Sequence Data
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis