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Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

DOI: 10.1038/s41467-020-17758-5 DOI Help

Authors: Rafael Nunez-ramirez (Centro de Investigaciones Biológicas Margarita Salas, CSIC) , Juanjo Huesa (Universitat de València) , Yolanda Bel (Universitat de València) , Juan Ferré (Universitat de València) , Patricia Casino (Universitat de València) , Ernesto Arias-palomo (Centro de Investigaciones Biológicas Margarita Salas, CSIC)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 11

State: Published (Approved)
Published: August 2020
Diamond Proposal Number(s): 21062 , 24924

Open Access Open Access

Abstract: Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. These proteins are produced as inactive protoxins that need to be activated by midgut proteases to trigger cell death. However, little is known about their three-dimensional organization and activation mechanism at the molecular level. Here, we have determined the structures of the protoxin and the protease-activated state of Vip3Aa at 2.9 Å using cryo-electron microscopy. The reconstructions show that the protoxin assembles into a pyramid-shaped tetramer with the C-terminal domains exposed to the solvent and the N-terminal region folded into a spring-loaded apex that, after protease activation, drastically remodels into an extended needle by a mechanism akin to that of influenza haemagglutinin. These results provide the molecular basis for Vip3 activation and function, and serves as a strong foundation for the development of more efficient insecticidal proteins.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios III-Titan Krios III at Diamond , Krios IV-Titan Krios IV at Diamond


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