ArticleMicrobial biotechnology2022
Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.
Article in Microbial biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 20 citations in OpenAlex.
- Lack of Tolerance Development Following Oral Exposure Tosublethal Cry1 and Vip3Aa Proteins inInsects · 2026Article
- Resistance to Vip3Aa: A Growing Threat with Unclear Mechanisms and Management Implications.Insects · 2025Review
- 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
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- N-Terminal α-Helices in Domain I ofToxins · 2024Article
- Domain IIIToxins · 2024Article
- Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.The Journal of biological chemistry · 2023Article
- Biomolecules in modern and sustainable agriculture.3 Biotech · 2023Review
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
- Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.Microbial biotechnology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vip3 proteins are produced by Bacillus thuringiensis and are toxic against lepidopterans, reason why the vip3Aa gene has been introduced into cotton and corn to control agricultural pests. Recently, the structure of Vip3 proteins has been determined and consists of a tetramer where each monomer is composed of five structural domains. The transition from protoxin to the trypsin-activated form involves a major conformational change of the N-terminal Domain I, which is remodelled into a tetrameric coiled-coil structure that is thought to insert into the apical membrane of the midgut cells. To better understand the relevance of this major change in Domain I for the insecticidal activity, we have generated several mutants aimed to alter the activity and remodelling capacity of this central region to understand its function. These mutants have been characterized by proteolytic processing, negative staining electron microscopy, and toxicity bioassays against Spodoptera exigua. The results show the crucial role of helix α1 for the insecticidal activity and in restraining the Domain I in the protoxin conformation, the importance of the remodelling of helices α2 and α3, the proteolytic processing that takes place between Domains I and II, and the role of the C-t Domains IV and V to sustain the conformational change necessary for toxicity.
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