Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)

Detalhes bibliográficos
Autor(a) principal: Bergamasco, V. B. [UNESP]
Data de Publicação: 2013
Outros Autores: Mendes, D. R P [UNESP], Fernandes, O. A. [UNESP], Desidério, J. A. [UNESP], Lemos, M. V F [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.jip.2012.11.011
http://hdl.handle.net/11449/74473
Resumo: The polyphagous pests belonging to the genus Spodoptera are considered to be among the most important causes of damage and are widely distributed throughout the Americas'. Due to the extensive use of genetically modified plants containing Bacillus thuringiensis genes that code for insecticidal proteins, resistant insects may arise. To prevent the development of resistance, pyramided plants, which express multiple insecticidal proteins that act through distinct mode of actions, can be used. This study analyzed the mechanisms of action for the proteins Cry1Ia10 and Vip3Aa on neonatal Spodoptera frugiperda, Spodoptera albula, Spodoptera eridania and Spodoptera cosmioides larvae. The interactions of these toxins with receptors on the intestinal epithelial membrane were also analyzed by binding biotinylated toxins to brush border membrane vesicles (BBMVs) from the intestines of these insects. A putative receptor of approximately 65. kDa was found by ligand blotting in all of these species. In vitro competition assays using biotinylated proteins have indicated that Vip3Aa and Cry1Ia10 do not compete for the same receptor for S. frugiperda, S. albula and S. cosmioides and that Vip3Aa was more efficient than Cry1Ia10 when tested individually, by bioassays. A synergistic effect of the toxins in S. frugiperda, S. albula and S. cosmioides was observed when they were combined. However, in S. eridania, Cry1Ia10 and Vip3Aa might compete for the same receptor and through bioassays Cry1Ia10 was more efficient than Vip3Aa and showed an antagonistic effect when the proteins were combined. These results suggest that using these genes to develop pyramided plants may not prove effective in preventing the development of resistance in S. eridiana. © 2012 Elsevier Inc.
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spelling Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)In vitro competition assaysReceptor bindingSpodoptera albulaSpodoptera cosmioidesSpodoptera eridaniaSpodoptera frugiperdaBacillus thuringiensisHexapodaLepidopteraSpodopteraThe polyphagous pests belonging to the genus Spodoptera are considered to be among the most important causes of damage and are widely distributed throughout the Americas'. Due to the extensive use of genetically modified plants containing Bacillus thuringiensis genes that code for insecticidal proteins, resistant insects may arise. To prevent the development of resistance, pyramided plants, which express multiple insecticidal proteins that act through distinct mode of actions, can be used. This study analyzed the mechanisms of action for the proteins Cry1Ia10 and Vip3Aa on neonatal Spodoptera frugiperda, Spodoptera albula, Spodoptera eridania and Spodoptera cosmioides larvae. The interactions of these toxins with receptors on the intestinal epithelial membrane were also analyzed by binding biotinylated toxins to brush border membrane vesicles (BBMVs) from the intestines of these insects. A putative receptor of approximately 65. kDa was found by ligand blotting in all of these species. In vitro competition assays using biotinylated proteins have indicated that Vip3Aa and Cry1Ia10 do not compete for the same receptor for S. frugiperda, S. albula and S. cosmioides and that Vip3Aa was more efficient than Cry1Ia10 when tested individually, by bioassays. A synergistic effect of the toxins in S. frugiperda, S. albula and S. cosmioides was observed when they were combined. However, in S. eridania, Cry1Ia10 and Vip3Aa might compete for the same receptor and through bioassays Cry1Ia10 was more efficient than Vip3Aa and showed an antagonistic effect when the proteins were combined. These results suggest that using these genes to develop pyramided plants may not prove effective in preventing the development of resistance in S. eridiana. © 2012 Elsevier Inc.Departamento de Biologia Aplicada à Agropecuária Universidade Estadual Paulista (UNESP) Faculdade de Ciências Agrárias e Veterinárias, Rod. Prof. Paulo Donato Castellane km 5, CEP 14884-900, Jaboticabal, SPDepartamento de Biologia Aplicada à Agropecuária Universidade Estadual Paulista (UNESP) Faculdade de Ciências Agrárias e Veterinárias, Rod. Prof. Paulo Donato Castellane km 5, CEP 14884-900, Jaboticabal, SPUniversidade Estadual Paulista (Unesp)Bergamasco, V. B. [UNESP]Mendes, D. R P [UNESP]Fernandes, O. A. [UNESP]Desidério, J. A. [UNESP]Lemos, M. V F [UNESP]2014-05-27T11:28:18Z2014-05-27T11:28:18Z2013-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article152-158application/pdfhttp://dx.doi.org/10.1016/j.jip.2012.11.011Journal of Invertebrate Pathology, v. 112, n. 2, p. 152-158, 2013.0022-20111096-0805http://hdl.handle.net/11449/7447310.1016/j.jip.2012.11.011WOS:0003143810000092-s2.0-848715950102-s2.0-84871595010.pdf145828828775788012950513405918367179273060624761Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Invertebrate Pathology2.5110,9290,929info:eu-repo/semantics/openAccess2024-06-06T13:05:10Zoai:repositorio.unesp.br:11449/74473Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T21:50:01.056087Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
title Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
spellingShingle Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
Bergamasco, V. B. [UNESP]
In vitro competition assays
Receptor binding
Spodoptera albula
Spodoptera cosmioides
Spodoptera eridania
Spodoptera frugiperda
Bacillus thuringiensis
Hexapoda
Lepidoptera
Spodoptera
title_short Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
title_full Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
title_fullStr Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
title_full_unstemmed Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
title_sort Bacillus thuringiensis Cry1Ia10 and Vip3Aa protein interactions and their toxicity in Spodoptera spp. (Lepidoptera)
author Bergamasco, V. B. [UNESP]
author_facet Bergamasco, V. B. [UNESP]
Mendes, D. R P [UNESP]
Fernandes, O. A. [UNESP]
Desidério, J. A. [UNESP]
Lemos, M. V F [UNESP]
author_role author
author2 Mendes, D. R P [UNESP]
Fernandes, O. A. [UNESP]
Desidério, J. A. [UNESP]
Lemos, M. V F [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Bergamasco, V. B. [UNESP]
Mendes, D. R P [UNESP]
Fernandes, O. A. [UNESP]
Desidério, J. A. [UNESP]
Lemos, M. V F [UNESP]
dc.subject.por.fl_str_mv In vitro competition assays
Receptor binding
Spodoptera albula
Spodoptera cosmioides
Spodoptera eridania
Spodoptera frugiperda
Bacillus thuringiensis
Hexapoda
Lepidoptera
Spodoptera
topic In vitro competition assays
Receptor binding
Spodoptera albula
Spodoptera cosmioides
Spodoptera eridania
Spodoptera frugiperda
Bacillus thuringiensis
Hexapoda
Lepidoptera
Spodoptera
description The polyphagous pests belonging to the genus Spodoptera are considered to be among the most important causes of damage and are widely distributed throughout the Americas'. Due to the extensive use of genetically modified plants containing Bacillus thuringiensis genes that code for insecticidal proteins, resistant insects may arise. To prevent the development of resistance, pyramided plants, which express multiple insecticidal proteins that act through distinct mode of actions, can be used. This study analyzed the mechanisms of action for the proteins Cry1Ia10 and Vip3Aa on neonatal Spodoptera frugiperda, Spodoptera albula, Spodoptera eridania and Spodoptera cosmioides larvae. The interactions of these toxins with receptors on the intestinal epithelial membrane were also analyzed by binding biotinylated toxins to brush border membrane vesicles (BBMVs) from the intestines of these insects. A putative receptor of approximately 65. kDa was found by ligand blotting in all of these species. In vitro competition assays using biotinylated proteins have indicated that Vip3Aa and Cry1Ia10 do not compete for the same receptor for S. frugiperda, S. albula and S. cosmioides and that Vip3Aa was more efficient than Cry1Ia10 when tested individually, by bioassays. A synergistic effect of the toxins in S. frugiperda, S. albula and S. cosmioides was observed when they were combined. However, in S. eridania, Cry1Ia10 and Vip3Aa might compete for the same receptor and through bioassays Cry1Ia10 was more efficient than Vip3Aa and showed an antagonistic effect when the proteins were combined. These results suggest that using these genes to develop pyramided plants may not prove effective in preventing the development of resistance in S. eridiana. © 2012 Elsevier Inc.
publishDate 2013
dc.date.none.fl_str_mv 2013-02-01
2014-05-27T11:28:18Z
2014-05-27T11:28:18Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.jip.2012.11.011
Journal of Invertebrate Pathology, v. 112, n. 2, p. 152-158, 2013.
0022-2011
1096-0805
http://hdl.handle.net/11449/74473
10.1016/j.jip.2012.11.011
WOS:000314381000009
2-s2.0-84871595010
2-s2.0-84871595010.pdf
1458288287757880
1295051340591836
7179273060624761
url http://dx.doi.org/10.1016/j.jip.2012.11.011
http://hdl.handle.net/11449/74473
identifier_str_mv Journal of Invertebrate Pathology, v. 112, n. 2, p. 152-158, 2013.
0022-2011
1096-0805
10.1016/j.jip.2012.11.011
WOS:000314381000009
2-s2.0-84871595010
2-s2.0-84871595010.pdf
1458288287757880
1295051340591836
7179273060624761
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Invertebrate Pathology
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dc.format.none.fl_str_mv 152-158
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
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reponame_str Repositório Institucional da UNESP
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repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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