ArticleScientific reports2018
Critical amino acids for the insecticidal activity of Vip3Af from Bacillus thuringiensis: Inference on structural aspects.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity.Biology · 2026Article
- Biophysical Analysis of Vip3Aa Toxin Mutants Before and After Activation.International journal of molecular sciences · 2024Article
- Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity.The Journal of biological chemistry · 2023Article
- Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.Microbial biotechnology · 2022Article
- In vivo competition assays between Vip3 proteins confirm the occurrence of shared binding sites in Spodoptera littoralis.Scientific reports · 2022Article
- Critical Domains in the Specific Binding of Radiolabeled Vip3Af Insecticidal Protein to Brush Border Membrane Vesicles fromApplied and environmental microbiology · 2021Article
- Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane.Nature communications · 2021Article
- Vegetative Insecticidal Protein (Vip): A Potential Contender FromFrontiers in microbiology · 2021Review
- Current Insights on Vegetative Insecticidal Proteins (Vip) as Next Generation Pest Killers.Toxins · 2020Review
- Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.Nature communications · 2020Article
- Structural and Functional Insights into the C-terminal Fragment of Insecticidal Vip3A Toxin ofToxins · 2020Article
- Oligomer Formation and Insecticidal Activity ofToxins · 2020Article
- Article
- Structural Domains of theToxins · 2019Article
- Modification of Vip3Ab1 C-Terminus Confers Broadened Plant Protection from Lepidopteran Pests.Toxins · 2019Article
- Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut ofToxins · 2019Article
- Characterization of Bacillus thuringiensis isolates by their insecticidal activity and their production of Cry and Vip3 proteins.PloS one · 2018Article
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4 authors.
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Abstract
Vip3 vegetative insecticidal proteins from Bacillus thuringiensis are an important tool for crop protection against caterpillar pests in IPM strategies. While there is wide consensus on their general mode of action, the details of their mode of action are not completely elucidated and their structure remains unknown. In this work the alanine scanning technique was performed on 558 out of the total of 788 amino acids of the Vip3Af1 protein. From the 558 residue substitutions, 19 impaired protein expression and other 19 substitutions severely compromised the insecticidal activity against Spodoptera frugiperda. The latter 19 substitutions mainly clustered in two regions of the protein sequence (amino acids 167-272 and amino acids 689-741). Most of these substitutions also decreased the activity to Agrotis segetum. The characterisation of the sensitivity to proteases of the mutant proteins displaying decreased insecticidal activity revealed 6 different band patterns as evaluated by SDS-PAGE. The study of the intrinsic fluorescence of most selected mutants revealed only slight shifts in the emission peak, likely indicating only minor changes in the tertiary structure. An in silico modelled 3D structure of Vip3Af1 is proposed for the first time.
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