Simple Summary Bacillus thuringiensis Vip3 proteins are useful in biological control because of their specificity and low cross-resistance with Cry proteins. Therefore, it is important to reveal the insecticidal activities of these proteins by enhancing their efficacy. In this study, we aimed to investigate the insecticidal activity of specific amino acid alterations in domains IV and V of the Vip3Aa90 protein. Four mutant constructs were generated by site-directed mutagenesis, but only two mutant proteins could be expressed, purified, and tested against three lepidopteran pests from the genera Spodoptera and Grapholita. Bioactivity assays showed that triple and quadruple mutants increased toxicity against Spodoptera littoralis. However, no increased insecticidal activity was observed for Spodoptera exigua and Grapholita molesta. The findings suggest that the effect of amino acid substitutions in the C-terminus of Vip3Aa is species-specific and, in some cases, may significantly increase toxicity against some lepidopteran species.
The comparison of adopter and non-adopter sample reveals three potential adoption inhibitor, security, data privacy, and portability, which underlines the importance of the technical and security perspectives for research investigating the adoption of technology.
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It is demonstrated that linker-free PROTACs can outperform traditional designs, marking a paradigm shift in PROTAC development for targeted protein degradation.
Pinal, a 16-billion-parameter foundation model that produces protein candidates from natural-language functional descriptions, supports natural language as a high-level interface for candidate generation in protein design, enabling programmable exploration with reduced reliance on manually specified structural or seque...
A new machine-learning framework aims to improve the success rate of computational protein design while moving away from results that reproduce sequences found in nature.