Specificity and efficacy of purified Bacillus thuringiensis proteins against agronomically important insects
Autor: | Pamela G. Marrone, John T. Greenplate, Roy L. Fuchs, Terry B. Stone, David A. Fischhoff, Steve R. Sims, Frederick J. Perlak, Susan C. MacIntosh, Penny L. Hunst |
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Rok vydání: | 1990 |
Předmět: |
Insecticides
media_common.quotation_subject Bacterial Toxins Bacillus thuringiensis Insect Microbiology Hemolysin Proteins chemistry.chemical_compound Bacterial Proteins Species Specificity Animals Pest Control Biological Ecology Evolution Behavior and Systematics media_common Larva Bacillaceae Bacillus thuringiensis Toxins biology fungi food and beverages Pesticide biology.organism_classification Bacillales Endotoxins chemistry Growth inhibition Bacteria |
Zdroj: | Journal of Invertebrate Pathology. 56:258-266 |
ISSN: | 0022-2011 |
DOI: | 10.1016/0022-2011(90)90109-j |
Popis: | The host range and relative efficacy of three purified Bacillus thuringiensis insect control proteins were determined against 17 different agronomically important insects representing five orders and one species of mite. The three B. thuringiensis proteins were single gene products from B. thuringiensis ssp. kurstaki HD-1 (CryIA(b)) and HD-73 (CryIA(c)), both lepidopteran-specific proteins, and B. thuringiensis ssp. tenebrionis (CryIIIA), a coleopteran-specific protein. Seven insects showed sensitivity to both B. thuringiensis ssp. kurstaki proteins, whereas only 1 of the 18 insects was sensitive to B. thuringiensis ssp. tenebrionis protein. The level of B. thuringiensis ssp. kurstaki protein required for 50% mortality (LC50) varied by 2000-fold for these 7 insects. A larval growth inhibition assay was developed to determine the amount of B. thuringiensis ssp. kurstaki protein required to inhibit larval growth by 50% (EC50). This extremely sensitive assay enabled detection of B. thuringiensis ssp. kurstaki HD-73 levels as low as 1 ng/ml. |
Databáze: | OpenAIRE |
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