6533b82ffe1ef96bd1295c60
RESEARCH PRODUCT
Binding of individual Bacillus thuringiensis Cry proteins to the olive moth Prays oleae (Lepidoptera: Yponomeutidae)
H. K. AldebisJuan FerréCarmen Sara Hernández-rodríguezEnrique Vargas-osunaSergio Pérez-guerrerosubject
InsecticidesBinding SitesBacillus thuringiensis Toxinsbiologymedia_common.quotation_subjectfungiBiological pest controlInsectMothsPrays oleaebiology.organism_classificationEndotoxinsLepidoptera genitaliaHemolysin ProteinsBiopesticideBacterial ProteinsCry1AcLarvaBacillus thuringiensisBotanyAnimalsPEST analysisPest Control BiologicalEcology Evolution Behavior and Systematicsmedia_commondescription
The microlepidopteran Prays oleae is one of the main insect pests causing significant crop losses in the Mediterranean olive groves. Bacillus thuringiensis based insecticides are being successfully used to minimize the impact of the second and third generations of this pest. However, because of its very small size and difficulty of rearing, very few studies have been carried out to determine the potency and mode of action of B. thuringiensis Cry proteins in this insect. In this study, Cry1Ac, Cry1Ca, and Cry1Fa proteins were shown to be toxic to third instar larvae of P. oleae. Furthermore, binding assays with (125)I-Cry1Ac and brush border membrane vesicles from midguts of last-instar larvae showed specific binding sites for Cry1Ac that are shared, with low affinity, by Cry1Ca and Cry1Fa.
year | journal | country | edition | language |
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2009-02-01 | Journal of Invertebrate Pathology |