ArticleThe Journal of biological chemistry2023
Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.
Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity.Biology · 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
- Interbacterial warfare in the human gut: insights from Bacteroidales' perspective.Gut microbes · 2025Review
- Resistance to Vip3Aa: A Growing Threat with Unclear Mechanisms and Management Implications.Insects · 2025Review
- 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
- A highly conserved SusCD transporter determines the import and species-specific antagonism of Bacteroides ubiquitin homologues.Nature communications · 2024Article
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- Domain IIIToxins · 2024Article
- Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome.Nature microbiology · 2024Article
- A strategy to enhance the insecticidal potency of Vip3Aa by introducing additional cleavage sites to increase its proteolytic activation efficiency.Engineering microbiology · 2023Article
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbially derived, protein-based biopesticides offer a more sustainable pest management alternative to synthetic pesticides. Vegetative insecticidal proteins (Vip3), multidomain proteins secreted by Bacillus thuringiensis, represent a second-generation insecticidal toxin that has been preliminarily used in transgenic crops. However, the molecular mechanism underlying Vip3's toxicity is poorly understood. Here, we determine the distinct functions and contributions of the domains of the Vip3Aa protein to its toxicity against Spodoptera frugiperda larvae. We demonstrate that Vip3Aa domains II and III (DII-DIII) bind the midgut epithelium, while DI is essential for Vip3Aa's stability and toxicity inside the protease-enriched host insect midgut. DI-DIII can be activated by midgut proteases and exhibits cytotoxicity similar to full-length Vip3Aa. In addition, we determine that DV can bind the peritrophic matrix via its glycan-binding activity, which contributes to Vip3Aa insecticidal activity. In summary, this study provides multiple insights into Vip3Aa's mode-of-action which should significantly facilitate the clarification of its insecticidal mechanism and its further rational development.
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