Cross-resistance of the diamondback moth indicates altered interactions with domain II of Bacillus thuringiensis toxins

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.

Observations, Insects, Toxins

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Different domains of Bacillus thuringiensis delta-endotoxins can bind to insect midgut membrane proteins on ligand blots

Article Abstract:

A study of the binding behavior of the constituent domains of CryIA(b) and CryIA(c) demonstrates interactions of insect membrane proteins with both domain II and III. Domain III of CryIA(b) and domains II and III of CryIA(c) bind to 205-kDa proteins of Spodoptera exigua blots and 210-kDa and 250-kDa proteins of Manduca sexta blots respectively, while other domains show no specific binding. CryIA(c) in M. sexta interacts with 210-kDa protein via domain I and/or domain II.

Protein binding

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Incorporation of protease K into larval insect membrane vesicles does not result in disruption of integrity or function of the pore-forming Bacillus thuringiensis delta-endotoxin

Article Abstract:

Results demonstrate that exposure of the delta-endotoxin from Bacillus thuringiensis to protease K does not affect the integrity or the function of the toxin as shown by intact aggregate and ion forming capabilities.

United States, Analysis, Usage, Proteases, Bacterial toxins, Structure-activity relationships (Biochemistry)

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