ArticleNature communications2021
Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- Structure of NO16, a marine non-tailed vibriophage with an unusual symmetry-mismatched vertex arrangement.PLoS pathogens · 2026Article
- Domain-guided engineering of a thermoresistant Vip3A toxin for enhanced functional robustness.Scientific reports · 2026Article
- Establishment of antibodies-based novel multi-modal highly sensitive immunoassay platforms for detecting Bacillus thuringiensis Vip3Aa toxin in agricultural samples.Analytical and bioanalytical chemistry · 2026Article
- Review
- Review
- Vip3C proteins fromApplied and environmental microbiology · 2025Article
- Insights into the structural changes that trigger receptor binding upon proteolytic activation of Bacillus thuringiensis Vip3Aa insecticidal protein.PLoS pathogens · 2024Article
- Biophysical Analysis of Vip3Aa Toxin Mutants Before and After Activation.International journal of molecular sciences · 2024Article
- Structural basis of α-latrotoxin transition to a cation-selective pore.Nature communications · 2024Article
- Article
- Protein Engineering of Vip3A in a Selected Bacillus thuringiensis Host for Consistent High Protein Production.Current microbiology · 2024Article
- iJAZ-based approach to engineer lepidopteran pest resistance in multiple crop species.Nature plants · 2024Article
- N-Terminal α-Helices in Domain I ofToxins · 2024Article
- Domain IIIToxins · 2024Article
- A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency.Engineering microbiology · 2023Article
- Channel Formation in Cry Toxins: An Alphafold-2 Perspective.International journal of molecular sciences · 2023Article
- Novel insecticidal proteins from ferns resemble insecticidal proteins fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.The Journal of biological chemistry · 2023Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Insect pests are a major cause of crop losses worldwide, with an estimated economic cost of $470 billion annually. Biotechnological tools have been introduced to control such insects without the need for chemical pesticides; for instance, the development of transgenic plants harbouring genes encoding insecticidal proteins. The Vip3 (vegetative insecticidal protein 3) family proteins from Bacillus thuringiensis convey toxicity to species within the Lepidoptera, and have wide potential applications in commercial agriculture. Vip3 proteins are proposed to exert their insecticidal activity through pore formation, though to date there is no mechanistic description of how this occurs on the membrane. Here we present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms in conjunction with structural and functional data on toxin-membrane interactions. Together these data demonstrate that activated Vip3Bc1 complex is able to insert into membranes in a highly efficient manner, indicating that receptor binding is the likely driver of Vip3 specificity.
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