ArticleNature communications2020
Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 107 citations in OpenAlex.
- Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity.Biology · 2026Article
- 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
- The transgenic Vip3A poplar plant confers high resistance against Hyphantria cunea Drury.Transgenic research · 2026Article
- Review
- Chemical defense mechanisms of soybean genotypes against lepidopterans.Frontiers in plant science · 2026Review
- Resistance to Vip3Aa: A Growing Threat with Unclear Mechanisms and Management Implications.Insects · 2025Review
- Vip3C proteins fromApplied and environmental microbiology · 2025Article
- Impact of codon optimization onFrontiers in plant science · 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
- Article
- N-Terminal α-Helices in Domain I ofToxins · 2024Article
- Domain IIIToxins · 2024Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. These proteins are produced as inactive protoxins that need to be activated by midgut proteases to trigger cell death. However, little is known about their three-dimensional organization and activation mechanism at the molecular level. Here, we have determined the structures of the protoxin and the protease-activated state of Vip3Aa at 2.9 Å using cryo-electron microscopy. The reconstructions show that the protoxin assembles into a pyramid-shaped tetramer with the C-terminal domains exposed to the solvent and the N-terminal region folded into a spring-loaded apex that, after protease activation, drastically remodels into an extended needle by a mechanism akin to that of influenza haemagglutinin. These results provide the molecular basis for Vip3 activation and function, and serves as a strong foundation for the development of more efficient insecticidal proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.