Novel Bacillus thuringiensis binary insecticidal crystal proteins active on western corn rootworm, Diabrotica virgifera virgifera LeConte
Autor: | Mark Knuth, Lisa Stamp, Brian A. Stockhoff, Kenneth E. Narva, Guy A. Cardineau, George E. Schwab, R. Tracy Ellis, Josh Russell, H. Ernest Schnepf |
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Rok vydání: | 2002 |
Předmět: |
Sequence analysis
Bacterial Toxins Molecular Sequence Data Bacillus thuringiensis Applied Microbiology and Biotechnology Bacillus sphaericus Zea mays Microbiology Hemolysin Proteins Bacterial Proteins Invertebrate Microbiology Animals Amino Acid Sequence Pest Control Biological Peptide sequence Bacillaceae Ecology biology Bacillus thuringiensis Toxins Base Sequence Sequence Analysis DNA biology.organism_classification Plants Genetically Modified Bacillales Coleoptera Endotoxins Open reading frame Western corn rootworm Food Science Biotechnology |
Zdroj: | Applied and environmental microbiology. 68(3) |
ISSN: | 0099-2240 |
Popis: | A new family of insecticidal crystal proteins was discovered by screening sporulated Bacillus thuringiensis cultures for oral activity against western corn rootworm (WCR) larvae. B. thuringiensis isolates PS80JJ1, PS149B1, and PS167H2 have WCR insecticidal activity attributable to parasporal inclusion bodies containing proteins with molecular masses of ca. 14 and 44 kDa. The genes encoding these polypeptides reside in apparent operons, and the 14-kDa protein open reading frame (ORF) precedes the 44-kDa protein ORF. Mutagenesis of either gene in the apparent operons dramatically reduced insecticidal activity of the corresponding recombinant B. thuringiensis strain. Bioassays performed with separately expressed, biochemically purified 14- and 44-kDa polypeptides also demonstrated that both proteins are required for WCR mortality. Sequence comparisons with other known B. thuringiensis insecticidal proteins failed to reveal homology with previously described Cry, Cyt, or Vip proteins. However, there is evidence that the 44-kDa polypeptide and the 41.9- and 51.4-kDa binary dipteran insecticidal proteins from Bacillus sphaericus are evolutionarily related. The 14- and 44-kDa polypeptides from isolates PS80JJ1, PS149B1, and PS167H2 have been designated Cry34Aa1, Cry34Ab1, and Cry34Ac1, respectively, and the 44-kDa polypeptides from these isolates have been designated Cry35Aa1, Cry35Ab1, and Cry35Ac1, respectively. |
Databáze: | OpenAIRE |
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