Article Abstract:
Analyses of responses to insecticidal crystal proteins (ICP) from Bacillus thuringiensis by a Cry 1A-resistant strain (NO-QA) and a susceptible strain (LAB-P), lead to the conclusion that resistance to Cry1A alters intersections between insects and domain 2. The interdependence of cross-resistance in strain NO-QA of the diamondback moth and amino acid sequence similarity among ICPs is greater for domain 2 than for domain 1 or 3. It is concluded that diamondback moth strain NO-QA cross-resistance extends beyond the Cry1A family to the families of Cry1F and Cry1J and to the protein H04.
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Article Abstract:
Laboratory selection improved the resistance to the Bacillus thuringiensis toxin Cry1C in a strain of diamondback moth Plutella xylostella. The selected strain was derived from a field population that had evolved high levels of resistance to Bacillus thuringiensis subsp. kurstaki and moderate resistance to Cry1C of the selected strain increased to 62-fold after six generations of selection. Analysis of F1 hybrid progeny from reciprocal crosses between the selected strain and susceptible strain indicated that the resistance to Cry1C was autosomally inherited.
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Article Abstract:
The 120-kDa Cry1Ac-binding aminopetidase N (APN) isolated from susceptible and resistant larvae of Plutella xylostella was analyzed to determine the presence of C-terminal glycosyl-phosphatidylinositol (GPI) anchors. Analysis of the purified toxin-binding APN from the brush border membrane vesicles (BBMV) of diamondback moth larvae indicated the presence of aminopeptidase activity. Furthermore, toxin binding to the BBMV of resistant larvae was absent due to GPI anchorage of APN and the presence of endogenous phosphatidylinositol-specific phospholipase C.
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