ArticleApplied and environmental microbiology2003
The mode of action of the Bacillus thuringiensis vegetative insecticidal protein Vip3A differs from that of Cry1Ab delta-endotoxin.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 315 citations in OpenAlex.
- Domain-guided engineering of a thermoresistant Vip3A toxin for enhanced functional robustness.Scientific reports · 2026Article
- Review
- A potent Vip3Aa94 protein from ThaiPeerJ · 2026Article
- Efficacy of Transgenic Maize LD05 Against Fall Armyworm (Plants (Basel, Switzerland) · 2025Article
- Resistance to Vip3Aa: A Growing Threat with Unclear Mechanisms and Management Implications.Insects · 2025Review
- Integrated genomic and proteomic analysis of local Bacillus thuringiensis isolates for targeted insect pest control and functional insight.Archives of microbiology · 2025Article
- Disruption of HaVipR1 confers Vip3Aa resistance in the moth crop pest Helicoverpa armigera.PLoS biology · 2025Article
- Transgenic soybean expressing Cry1Ab-Vip3A fusion protein confers broad-spectrum resistance to lepidopteran pest.Plant cell reports · 2025Article
- Biophysical Analysis of Vip3Aa Toxin Mutants Before and After Activation.International journal of molecular sciences · 2024Article
- Retrotransposon-mediated disruption of a chitin synthase gene confers insect resistance to Bacillus thuringiensis Vip3Aa toxin.PLoS biology · 2024Article
- Review
- Protein Engineering of Vip3A in a Selected Bacillus thuringiensis Host for Consistent High Protein Production.Current microbiology · 2024Article
- Domain IIIToxins · 2024Article
- Reduced toxin binding associated with resistance to Vip3Aa in the corn earworm (Applied and environmental microbiology · 2023Article
- An Extended Investigation of UnexpectedToxins · 2023Article
- Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.The Journal of biological chemistry · 2023Article
- Molecular Characterization and Efficacy Evaluation of Transgenic Maize HarboringPlants (Basel, Switzerland) · 2023Article
- PHB2 affects the virulence of Vip3Aa to Sf9 cells through internalization and mitochondrial stability.Virulence · 2022Article
- Impact of Temperature Change on the Fall Armyworm,Insects · 2022Review
- Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.Microbial biotechnology · 2022Article
46 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Vip3A protein, secreted by Bacillus spp. during the vegetative stage of growth, represents a new family of insecticidal proteins. In our investigation of the mode of action of Vip3A, the 88-kDa Vip3A full-length toxin (Vip3A-F) was proteolytically activated to an approximately 62-kDa core toxin either by trypsin (Vip3A-T) or lepidopteran gut juice extracts (Vip3A-G). Biotinylated Vip3A-G demonstrated competitive binding to lepidopteran midgut brush border membrane vesicles (BBMV). Furthermore, in ligand blotting experiments with BBMV from the tobacco hornworm, Manduca sexta (Linnaeus), activated Cry1Ab bound to 120-kDa aminopeptidase N (APN)-like and 250-kDa cadherin-like molecules, whereas Vip3A-G bound to 80-kDa and 100-kDa molecules which are distinct from the known Cry1Ab receptors. In addition, separate blotting experiments with Vip3A-G did not show binding to isolated Cry1A receptors, such as M. sexta APN protein, or a cadherin Cry1Ab ecto-binding domain. In voltage clamping assays with dissected midgut from the susceptible insect, M. sexta, Vip3A-G clearly formed pores, whereas Vip3A-F was incapable of pore formation. In the same assay, Vip3A-G was incapable of forming pores with larvae of the nonsusceptible insect, monarch butterfly, Danaus plexippus (Linnaeus). In planar lipid bilayers, both Vip3A-G and Vip3A-T formed stable ion channels in the absence of any receptors, supporting pore formation as an inherent property of Vip3A. Both Cry1Ab and Vip3A channels were voltage independent and highly cation selective; however, they differed considerably in their principal conductance state and cation specificity. The mode of action of Vip3A supports its use as a novel insecticidal agent.
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