Canadian Forest Service Publications

Interaction between Cry9Ca and two Cry1A delta-endotoxins from Bacillus thuringiensis in larval toxicity and binding to brush border membrane vesicles of the spruce budworm, Choristoneura fumiferana Clemens. 2002. Pang, A.S.D.; Gringorten, J.L.; van Frankenhuyzen, K. FEMS Microbiology Letters 215: 109-114.

Year: 2002

Issued by: Great Lakes Forestry Centre

Catalog ID: 24413

Language: English

Availability: PDF (request by e-mail)

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A genetically altered variant of Cry9Ca from _Choristoneura fumiferana Clemens. Its activity, as measured by feeding inhibition in frass-failure assays, is estimated to be four to seven times greater than B. thuringiensis subsp. kurstaki HD-1, the strain currently used in commercial products to control this insect. Bioassays against budworm of mixtures of the modified Cry9Ca and two of the Cry1A endotoxin proteins produced by HD-1 show neither synergism nor antagonism. Experiments with brush border membrane vesicles from budworm midgut revealed that Cry9Ca and the Cry1A toxins share a common binding site and that bound Cry9Ca can be displaced from the membrane to some extent by the Cry1A toxins. However, it is uncertain whether the binding site is actually the receptor molecule or a membrane protein associated with pore formation.