ArticlePloS one2021
Bacillus thuringiensis chimeric proteins Cry1A.2 and Cry1B.2 to control soybean lepidopteran pests: New domain combinations enhance insecticidal spectrum of activity and novel receptor contributions.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Field performance of MON 94637 and laboratory evidence supporting a Bt pyramiding strategy against key lepidopteran pests in Brazil.Pest management science · 2026Article
- Article
- Characterization of the spectrum of insecticidal activity of Cry1B.3, Cry1Da_7, and Vip3Cb1 proteins produced by lepidopteran-protected MON 89151 cotton.Scientific reports · 2025Article
- Ecological risk assessment for Cry1Da_7, Cry1B.3 and Vip3Cb1 proteins expressed in MON 89151 cotton: an insect-protected cotton with targeted activity against Lepidoptera.Transgenic research · 2025Article
- Distribution ofInsects · 2025Article
- Bioactive Potential of SomeInsects · 2024Article
- High-throughput screening for novelJournal of pesticide science · 2024Article
- Novel insecticidal proteins from ferns resemble insecticidal proteins fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Engineered chimeric insecticidal crystalline protein improves resistance to lepidopteran insects in rice (Oryza sativa L.) and maize (Zea mays L.).Scientific reports · 2022Article
- Engineering ofJournal of pesticide science · 2022Article
- In vivo competition assays between Vip3 proteins confirm the occurrence of shared binding sites in Spodoptera littoralis.Scientific reports · 2022Article
- Resistance status of lepidopteran soybean pests following large-scale use of MON 87701 × MON 89788 soybean in Brazil.Scientific reports · 2021Article
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Authors and funding
14 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two new chimeric Bacillus thuringiensis (Bt) proteins, Cry1A.2 and Cry1B.2, were constructed using specific domains, which provide insecticidal activity against key lepidopteran soybean pests while minimizing receptor overlaps between themselves, current, and soon to be commercialized plant incorporated protectants (PIP's) in soybean. Results from insect diet bioassays demonstrate that the recombinant Cry1A.2 and Cry1B.2 are toxic to soybean looper (SBL) Chrysodeixis includens Walker, velvetbean caterpillar (VBC) Anticarsia gemmatalis Hubner, southern armyworm (SAW) Spodoptera eridania, and black armyworm (BLAW) Spodoptera cosmioides with LC50 values < 3,448 ng/cm2. Cry1B.2 is of moderate activity with significant mortality and stunting at > 3,448 ng/cm2, while Cry1A.2 lacks toxicity against old-world bollworm (OWB) Helicoverpa armigera. Results from disabled insecticidal protein (DIP) bioassays suggest that receptor utilization of Cry1A.2 and Cry1B.2 proteins are distinct from each other and from current, and yet to be commercially available, Bt proteins in soy such as Cry1Ac, Cry1A.105, Cry1F.842, Cry2Ab2 and Vip3A. However, as Cry1A.2 contains a domain common to at least one commercial soybean Bt protein, resistance to this common domain in a current commercial soybean Bt protein could possibly confer at least partial cross resistance to Cry1A2. Therefore, Cry1A.2 and Cry1B.2 should provide two new tools for controlling many of the major soybean insect pests described above.
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