AI Article Synopsis
- A crystal-spore suspension of PS201T6 is toxic to Diprion similis larvae, likely due to the Cyt1Ba crystal protein.
- In a field experiment, PS201T6 decreased the survival and growth of D. similis over two weeks.
- Cyt1Ba demonstrates a wide range of insecticidal effects, impacting insects from four different orders, making it the most broadly effective Bacillus thuringiensis crystal protein identified so far.
Article 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.
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| http://dx.doi.org/10.1016/j.jip.2013.03.007 | DOI Listing |
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