Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane

Byrne, Matthew J., Iadanza, Matthew G., Arribas Perez, Marcos, Maskell, Daniel P., George, Rachel M., Hesketh, Emma L., Beales, Paul A., Zack, Marc D., Berry, Colin ORCID: https://orcid.org/0000-0002-9943-548X and Thompson, Rebecca F. 2021. Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane. Nature Communications 12 , 2791. 10.1038/s41467-021-23146-4

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Abstract

Insect pests are a major cause of crop losses worldwide, with an estimated economic cost of $470 billion annually. Biotechnological tools have been introduced to control such insects without the need for chemical pesticides; for instance, the development of transgenic plants harbouring genes encoding insecticidal proteins. The Vip3 (vegetative insecticidal protein 3) family proteins from Bacillus thuringiensis convey toxicity to species within the Lepidoptera, and have wide potential applications in commercial agriculture. Vip3 proteins are proposed to exert their insecticidal activity through pore formation, though to date there is no mechanistic description of how this occurs on the membrane. Here we present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms in conjunction with structural and functional data on toxin–membrane interactions. Together these data demonstrate that activated Vip3Bc1 complex is able to insert into membranes in a highly efficient manner, indicating that receptor binding is the likely driver of Vip3 specificity.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Additional Information:	This article is licensed under a Creative Commons Attribution 4.0 International License
Publisher:	Nature Research
ISSN:	2041-1723
Date of First Compliant Deposit:	31 March 2021
Date of Acceptance:	25 March 2021
Last Modified:	05 May 2023 06:25
URI:	https://orca.cardiff.ac.uk/id/eprint/140216

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