2024-03-28T22:55:11Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/2180062021-12-27T16:42:06Zcom_10261_86com_10261_1col_10261_339
DIGITAL.CSIC
author
Núñez-Ramírez, Rafael
author
Huesa, Juanjo
author
Bel, Yolanda
author
Ferré, Juan
author
Casino, Patricia
author
Arias-Palomo, Ernesto
funder
Ministerio de Economía y Competitividad (España)
funder
Ministerio de Ciencia, Innovación y Universidades (España)
orcid
Bel, Yolanda [0000-0002-6367-9220]
orcid
Ferré, Juan [0000-0001-5535-0612]
orcid
Casino, Patricia [0000-0002-2144-188X]
orcid
Arias-Palomo, Ernesto [0000-0002-2706-7411]
2020-08-14T12:00:55Z
2020-08-14T12:00:55Z
2020-08-07
Nature communications 11 (1) 3974 (2020)
http://hdl.handle.net/10261/218006
10.1038/s41467-020-17758-5
2041-1723
http://dx.doi.org/10.13039/501100003329
32769995
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.
eng
openAccess
Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis
artículo
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URL
https://digital.csic.es/bitstream/10261/218006/1/Nature%20Communications_n%c3%ba%c3%b1ez-Ram%c3%adrez_2020.pdf
File
MD5
3f0d7baa827f100c6d69393a14ae8f43
3975198
application/pdf
Nature Communications_núñez-Ramírez_2020.pdf