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Amino Acid Substitutions in the C-Terminal Domains of Vip3Aa Enhance Insecticidal Toxicity

Sep 2026 · Biology · Vol 15 · 0 citations · 26 references
Medicine

Abstract

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.

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