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Bacillus thuringiensis Cry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms, Spodoptera frugiperda (J.E. Smith)
Author(s) -
Yanfei Wang,
Jinling Wang,
Xiaoran Fu,
Jeffrey R. Nageotte,
JENNIFER SILVERMAN,
Eric C. Bretsnyder,
Danqi Chen,
T.J. Rydel,
Gregory J. Bean,
Ke Sherry Li,
Edward Kraft,
Anilkumar Gowda,
Autumn M. Nance,
Robert G. Moore,
Michael Pleau,
Jason S. Milligan,
Heather M. Anderson,
Peter Asiimwe,
A. Evans,
William J. Moar,
Samuel Martinelli,
Graham Head,
Jeffrey A. Haas,
James A. Baum,
Fei Yang,
David L. Kerns,
Agoston Jerga
Publication year - 2019
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00579-19
Subject(s) - spodoptera , bacillus thuringiensis , fall armyworm , biology , bioassay , insect , receptor , microbiology and biotechnology , botany , gene , biochemistry , bacteria , genetics , recombinant dna
There is increased concern with the development of resistance to insecticidal proteins currently expressed in crop plants, especially against high-resistance-risk pests such as fall armyworm (FAW), Spodoptera frugiperda , a maize pest that already has developed resistance to Bacillus thuringiensis ( Bt ) proteins such as Cry1F. Lepidopteran-specific proteins that bind new insect receptors will be critical in managing current Cry1F-resistant FAW and delaying future resistance development. Results from resistant insect assays, disabled insecticidal protein (DIP) bioassays, and cell-based assays using insect cells expressing individual receptors demonstrate that target receptors of the Cry1Da_7 and Cry1B.868 proteins are different from each other and from those of commercially available Bt proteins such as Cry1F, Cry1A.105, Cry2Ab, and Vip3A. Therefore, pyramiding these two new proteins in maize will provide durable control of this economically important pest in production agriculture.

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