Canadian Forest Service Publications

Activity of Bacillus thuringiensis cytlBa crystal protein against hymenopteran forest pests. 2013. van Frankenhuyzen, K.; Tonon, A. Journal of Invertebrate Pathology. 113:160-162.

Year: 2013

Available from: Great Lakes Forestry Centre

Catalog ID: 34672

Language: English

CFS Availability: PDF (request by e-mail)

Abstract

A crystal-spore suspension of PS201T6 was toxic to larvae of Diprion similis (Hymenoptera: Diprionidae). Toxicity was at least in part attributable to the Cyt1Ba crystal protein, as demonstrated by bioassays of solubilized protein produced by Escherichia coli expressing PS201T6's cyt1Ba gene. PS201T6 reduced survival and growth of D. similis in a 2-week field experiment. In laboratory bioassays, both toxin and parental strain affected Acantholyda erythrocephala (Pamphiliidae), Pikonema alaskensis (Tenthredinidae), and Neodiprion sertifer (Diprionidae), as well as spruce budworm, Choristoneura fumiferana (Lepidoptera: Tortricidae). Affecting insects across at least four orders (Diptera, Coleoptera, Hymenoptera, Lepidoptera), Cyt1Ba has the broadest insecticidal activity spectrum among Bacillus thuringiensis crystal proteins documented to date.

Plain Language Summary

: A crystal–spore suspension of PS201T6 was toxic to larvae of the introduced pine sawfly (Diprion similis). Toxicity was at least in part attributable to the Cyt1Ba crystal protein, as demonstrated by bioassays of solubilized protein produced by Escherichia coli expressing PS201T6’s cyt1Ba gene. PS201T6 reduced survival and growth of D. similis in a 2-week field experiment. In laboratory bioassays, both toxin and parental strain affected pine false webworm, yellowheaded spruce sawfly and European pine sawfly, as well as spruce budworm. Cyt1Ba has the broadest insecticidal activity spectrum among Bacillus thuringiensis crystal proteins documented to date affecting insects across at least four orders (Diptera, Coleoptera, Hymenoptera, Lepidoptera).

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