0000000000248338
AUTHOR
José L. Ménsua
Survival of two strains of Phthorimaea operculella (Lepidoptera: Gelechiidae) reared on transgenic potatoes expressing a Bacillus thuringiensis crystal protein
[Otros] Survie de deux souches de Phthorimaea operculella (Lepidoptera : Gelechiidae) élevées sur des pommes de terre transgéniques exprimant la protéine CrylAb de Bacillus thuringiensis. Deux populations de Phthorimaea operculella (Zeller), l'une supposée résistante au DipelTM (une préparation commerciale de delta-endotoxines de Bacillus thuringiensis) et l'autre sensible, ont été cultivées sur quatre cultivars de pomme de terre, deux transgéniques de première génération, exprimant la protéine CrylAb de Bacillus thuringiensis, et deux non transformés. La population de papillons considérée comme résistante a présenté une mortalité inférieure à celle de l'autre population, mais n'était pas v…
Global variation in the genetic and biochemical basis of diamondback moth resistance to Bacillus thuringiensis
Insecticidal proteins from the soil bacterium Bacillus thuringiensis (Bt) are becoming a cornerstone of ecologically sound pest management. However, if pests quickly adapt, the benefits of environmentally benign Bt toxins in sprays and genetically engineered crops will be short-lived. The diamondback moth ( Plutella xylostella ) is the first insect to evolve resistance to Bt in open-field populations. Here we report that populations from Hawaii and Pennsylvania share a genetic locus at which a recessive mutation associated with reduced toxin binding confers extremely high resistance to four Bt toxins. In contrast, resistance in a population from the Philippines shows multilocus control, a …
Pigment patterns in mutants affecting the biosynthesis of pteridines and xanthommatin in Drosophila melanogaster.
Eye-color mutants of Drosophila melanogaster have been analyzed for their pigment content and related metabolites. Xanthommatin and dihydroxanthommatin (pigments causing brown eye color) were measured after selective extraction in acidified butanol. Pteridines (pigments causing red eye color) were quantitated after separation of 28 spots by thin-layer chromatography, most of which are pteridines and a few of which are fluorescent metabolites from the xanthommatin pathway. Pigment patterns have been studied in 45 loci. The pteridine pathway ramifies into two double branches giving rise to isoxanthopterin, “drosopterins,” and biopterin as final products. The regulatory relationship among the …
Lack of cross‐resistance to otherBacillus thuringiensiscrystal proteins in a population ofPlutella xylostellahighly resistant to cryia(b)
Competition experiments were performed with brush border membrane vesicles of diamondback moth larvae using 125I‐labelled CryIA(b) and unlabelled CryIA(a), CryIA(b) and CryIA(c). The results suggested a model with a single binding site for CryIA(b). Heterologous competition showed that CryIA(c) competed as effectively as CryIA(b) for the CryIA(b) binding site, whereas CryIA(a) competed less effectively. Toxicity tests were performed on third instar larvae with trypsin‐activated insecticidal crystal proteins (ICPs) and a commercial formulation of Bacillus thuringiensis (Bt) (Dipel). A laboratory colony was found to be susceptible to all four ICPs tested and to Dipel. CryIA(b), CryIA(c) and C…
Role of Bacillus thuringiensis Toxin Domains in Toxicity and Receptor Binding in the Diamondback Moth
ABSTRACT The toxic fragment of Bacillus thuringiensis crystal proteins consists of three distinct structural domains. There is evidence that domain I is involved in pore formation and that domain II is involved in receptor binding and specificity. It has been found that, in some cases, domain III is also important in determining specificity. Furthermore, involvement of domain III in binding has also been reported recently. To investigate the role of toxin domains in the diamondback moth ( Plutella xylostella ), we used hybrid toxins with domain III substitutions among Cry1C, Cry1E, and Cry1Ab. Neither Cry1E nor G27 (a hybrid with domains I and II from Cry1E and domain III from Cry1C) was to…