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Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis

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Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis

dc.contributor.author	Lázaro-Berenguer, María
dc.contributor.author	Paredes-Martínez, Francisco
dc.contributor.author	Bel Cortés, Yolanda
dc.contributor.author	Núñez-Ramírez, Rafael
dc.contributor.author	Arias-Palomo, Ernesto
dc.contributor.author	Casino Ferrando, Patricia
dc.contributor.author	Ferré Manzanero, Juan
dc.date.accessioned	2022-12-07T14:31:31Z
dc.date.available	2022-12-07T14:31:31Z
dc.date.issued	2022
dc.identifier.citation	Lázaro-Berenguer, María Paredes-Martínez, Francisco Bel Cortés, Yolanda Núñez-Ramírez, Rafael Arias-Palomo, Ernesto Casino Ferrando, Patricia Ferré Manzanero, Juan 2022 Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis Microbial Biotechnology 15 10 2607 2618
dc.identifier.uri	https://hdl.handle.net/10550/84688
dc.description.abstract	Vip3 proteins are produced by Bacillus thuringiensis and are toxic against lepidopterans, reason why the vip3Aa gene has been introduced into cotton and corn to control agricultural pests. Recently, the structure of Vip3 proteins has been determined and consists of a tetramer where each monomer is composed of five structural domains. The transition from protoxin to the trypsin-activated form involves a major conformational change of the N-terminal Domain I, which is remodelled into a tetrameric coiled-coil structure that is thought to insert into the apical membrane of the midgut cells. To better understand the relevance of this major change in Domain I for the insecticidal activity, we have generated several mutants aimed to alter the activity and remodelling capacity of this central region to understand its function. These mutants have been characterized by proteolytic processing, negative staining electron microscopy, and toxicity bioassays against Spodoptera exigua. The results show the crucial role of helix α1 for the insecticidal activity and in restraining the Domain I in the protoxin conformation, the importance of the remodelling of helices α2 and α3, the proteolytic processing that takes place between Domains I and II, and the role of the C-t Domains IV and V to sustain the conformational change necessary for toxicity.
dc.language.iso	eng
dc.relation.ispartof	Microbial Biotechnology, 2022, vol. 15, num. 10, p. 2607-2618
dc.subject	Insecticides
dc.subject	Proteïnes
dc.subject	Biotecnologia
dc.title	Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis
dc.type	journal article	es_ES
dc.date.updated	2022-12-07T14:31:31Z
dc.identifier.doi	10.1111/1751-7915.14110
dc.identifier.idgrec	155692
dc.rights.accessRights	open access	es_ES