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dc.creatorGomis Cebolla, Joaquínes_ES
dc.creatorSantos, Rafael Ferreira doses_ES
dc.creatorWang, Yueqines_ES
dc.creatorCaballero Sánchez, Javieres_ES
dc.creatorCaballero Murillo, Primitivoes_ES
dc.creatorHe, Kanglaies_ES
dc.creatorJurat Fuentes, Juan Luises_ES
dc.creatorFerré, Juanes_ES
dc.date.accessioned2020-05-21T09:23:45Z
dc.date.available2020-05-21T09:23:45Z
dc.date.issued2020
dc.identifier.issn2072-6651
dc.identifier.urihttps://hdl.handle.net/2454/36959
dc.description.abstractThe bacterium Bacillus thuringiensis produces insecticidal Vip3 proteins during the vegetative growth phase with activity against several lepidopteran pests. To date, three different Vip3 protein families have been identified based on sequence identity: Vip3A, Vip3B, and Vip3C. In this study, we report the construction of chimeras by exchanging domains between Vip3Aa and Vip3Ca, two proteins with marked specificity differences against lepidopteran pests. We found that some domain combinations made proteins insoluble or prone to degradation by trypsin as most abundant insect gut protease. The soluble and trypsin-stable chimeras, along with the parental proteins Vip3Aa and Vip3Ca, were tested against lepidopteran pests from different continents: Spodoptera exigua, Spodoptera littoralis, Spodoptera frugiperda, Helicoverpa armigera, Mamestra brassicae, Anticarsia gemmatalis, and Ostrinia furnacalis. The exchange of the Nt domain (188 N-terminal amino acids) had little effect on the stability and toxicity (equal or slightly lower) of the resulting chimeric protein against all insects except for S. frugiperda, for which the chimera with the Nt domain from Vip3Aa and the rest of the protein from Vip3Ca showed a significant increase in toxicity compared to the parental Vip3Ca. Chimeras with the C-terminal domain from Vip3Aa (from amino acid 510 of Vip3Aa to the Ct) with the central domain of Vip3Ca (amino acids 189–509 based on the Vip3Aa sequence) made proteins that could not be solubilized. Finally, the chimera including the Ct domain of Vip3Ca and the Nt and central domain from Vip3Aa was unstable. Importantly, an insect species tolerant to Vip3Aa but susceptible to Vip3Ca, such as Ostrinia furnacalis, was also susceptible to chimeras maintaining the Ct domain from Vip3Ca, in agreement with the hypothesis that the Ct region of the protein is the one conferring specificity to Vip3 proteins.en
dc.description.sponsorshipThis research was supported to JF by the Spanish Ministry of Economy and Competitivity (Grants Ref. AGL2015‐70584‐C02‐1‐R and RTI2018‐095204‐B‐C21), by the Generalitat Valenciana (GVPROMETEOII‐2015‐ 001), and by European FEDER funds. JGC was recipient of a PhD grant from the Spanish Ministry of Economy and Competitivity (grant ref. BES‐2013‐065848 and EEBB‐I‐17‐12367). Support was also provided to JLJ‐F by an Agriculture and Food Research Initiative Foundational Program competitive grant (No. 2018‐67013‐27820) from the USDA National Institute of Food and Agriculture, and to KH by a grant 'Key Project for Breeding Genetically Modified Organisms' from China (grant ref. 2016ZX08003‐001).en
dc.format.extent15 p.
dc.format.mimetypeapplication/pdfen
dc.language.isoengen
dc.publisherMDPIen
dc.relation.ispartofToxins, 2020, 12 (2), 99en
dc.rights© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBacillus thuringiensisen
dc.subjectSpodoptera spp.en
dc.subjectHelicoverpa armigeraen
dc.subjectMamestra brassicaeen
dc.subjectAnticarsia gemmatalisen
dc.subjectOstrinia furnacalisen
dc.titleDomain shuffling between Vip3Aa and Vip3Ca: chimera stability and insecticidal activity against European, American, African, and Asian pestsen
dc.typeinfo:eu-repo/semantics/articleen
dc.typeArtículo / Artikuluaes
dc.contributor.departmentInstitute for Multidisciplinary Research in Applied Biology - IMABes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.identifier.doi10.3390/toxins12020099
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//AGL2015-70584-C2-2-R/ES/en
dc.relation.publisherversionhttps://doi.org/10.3390/toxins12020099
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dc.type.versionVersión publicada / Argitaratu den bertsioaes


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© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access
article distributed under the terms and conditions of the Creative Commons Attribution
(CC BY) license.
Except where otherwise noted, this item's license is described as © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.

El Repositorio ha recibido la ayuda de la Fundación Española para la Ciencia y la Tecnología para la realización de actividades en el ámbito del fomento de la investigación científica de excelencia, en la Línea 2. Repositorios institucionales (convocatoria 2020-2021).
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