Abstract

Vegetative insecticidal proteins (Vips) from Bacillus thuringiensis (Bt) are unique from crystal (Cry) proteins found in Bt parasporal inclusions as they are secreted during the bacterial vegetative growth phase and bind unique receptors to exert their insecticidal effects. We previously demonstrated that large modifications of the Vip3 C-terminus could redirect insecticidal spectrum but results in an unstable protein with no lethal activity. In the present work, we have generated a new Vip3 protein, Vip3Ab1-740, via modest modification of the Vip3Ab1 C-terminus. Vip3Ab1-740 is readily processed by midgut fluid enzymes and has lethal activity towards Spodoptera eridania, which is not observed with the Vip3Ab1 parent protein. Importantly, Vip3Ab1-740 does retain the lethal activity of Vip3Ab1 against other important lepidopteran pests. Furthermore, transgenic plants expressing Vip3Ab1-740 are protected against S. eridania, Spodoptera frugiperda, Helicoverpa zea, and Pseudoplusia includens. Thus, these studies demonstrate successful engineering of Vip3 proteins at the C-terminus to broaden insecticidal spectrum, which can be employed for functional expression in planta.

Highlights

  • Vegetative insecticidal proteins (Vips) have earned an important role in modern agriculture due to their ability to control lepidopteran pests that damage crops and impact yield

  • Vip proteins are produced during the vegetative growth phase of Bacillus thuringiensis (Bt), the same soil dwelling bacterium that produce delta endotoxins found in crystalline parasporal inclusions, known as

  • Vip3A protein can confer a lethal activity against previously non-susceptible insects

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Summary

Introduction

Vegetative insecticidal proteins (Vips) have earned an important role in modern agriculture due to their ability to control lepidopteran pests that damage crops and impact yield. As their name indicates, Vip proteins are produced during the vegetative growth phase of Bacillus thuringiensis (Bt), the same soil dwelling bacterium that produce delta endotoxins found in crystalline parasporal inclusions, known as. Vip3A proteins represent a mode of action different to Cry proteins in commercial cotton and corn crops [5] Since their identification in 1996 [6], Vip research has focused on the characterization of novel Vip proteins and their function [7]. The overwhelming majority of investigative work has Toxins 2019, 11, 316; doi:10.3390/toxins11060316 www.mdpi.com/journal/toxins

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