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  • Title: Bacillus thuringiensis crystal proteins CRY1Ab and CRY1Fa share a high affinity binding site in Plutella xylostella (L.).
    Author: Granero F, Ballester V, Ferré J.
    Journal: Biochem Biophys Res Commun; 1996 Jul 25; 224(3):779-83. PubMed ID: 8713122.
    Abstract:
    The future success of Bacillus thuringiensis based insecticides depends in part on our ability to prevent insects from developing resistance against their insecticidal crystal proteins. Two recent papers indicated cross-resistance between Cry1A proteins and Cry1Fa in two different insect species (Tabashnik et al., 1994, Appl. Environ. Microbiol. 60, 4627-4629; Gould et al., 1995, J. Econ. Entomol. 88, 1545-1559). Brush border membrane vesicles were prepared from Plutella xylostella and used in binding assays with 125I-labeled trypsin-activated crystal proteins. Competition experiments showed that Cry1Fa competed with Cry1Ab for a same binding site, though the latter still bound to a different minor binding site with apparently the same affinity. Cry1Ca did not compete for Cry1Ab binding sites nor Cry1Fa for Cry1Ca binding sites. Based on these results, a modification of the receptor shared by Cry1Ab and Cry1Fa might confer multiple resistance to Cry1A and Cry1Fa proteins.
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