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

Matthew J. Byrne, Matthew G. Iadanza, Marcos Arribas Perez, Daniel P. Maskell, Rachel M. George, Emma L. Hesketh, Paul A. Beales, Marc D. Zack, Colin Berry () and Rebecca F. Thompson ()
Additional contact information
Matthew J. Byrne: University of Leeds
Matthew G. Iadanza: University of Leeds
Marcos Arribas Perez: University of Leeds
Daniel P. Maskell: University of Leeds
Rachel M. George: University of Leeds
Emma L. Hesketh: University of Leeds
Paul A. Beales: University of Leeds
Marc D. Zack: Corteva Agriscience
Colin Berry: Cardiff School of Biosciences, Cardiff University
Rebecca F. Thompson: University of Leeds

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: 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.

Date: 2021
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-23146-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23146-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-23146-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().