Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein

Autores
Gomis-Cebolla, Joaquín; Ruiz de Escudero, Iñigo; Vera-Velasco, Natalia Mara; Hernández-Martínez, Patricia; Hernández-Rodríguez, Carmen Sara; Ceballos, Tomás; Palma, Leopoldo; Escriche, Baltasar; Caballero, Primitivo; Ferré, Juan
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately susceptible), Agrotis ipsilon and Ostrinia nubilalis (slightly susceptible). Processing Vip3Ca by O. nubilalis or M. brassicae midgut juice did not significantly changed its toxicity to either insect species, indicating that the low susceptibility of O. nubilalis is not due to a problem in the midgut processing of the toxin. M. brassicae larvae fed with Vip3Ca showed binding of this toxin to the apical membrane of the midgut epithelial cells. Histopathological inspection showed sloughing of the epithelial cells with further disruption, which suggests that the mode of action of Vip3Ca is similar to that described for Vip3Aa. Biotin-labeled Vip3Ca and Vip3Aa bound specifically to M. brassicae brush border membrane vesicles and both toxins competed for binding sites. This result suggests that insects resistant to Vip3A may also be cross-resistant to Vip3C, which has implications for Insect Resistance Management (IRM).
Fil: Gomis-Cebolla, Joaquín. Universidad de Valencia; España
Fil: Ruiz de Escudero, Iñigo. Universidad Publica de Navarra; España
Fil: Vera-Velasco, Natalia Mara. Universidad de Valencia; España
Fil: Hernández-Martínez, Patricia. Universidad de Valencia; España
Fil: Hernández-Rodríguez, Carmen Sara. Universidad de Valencia; España
Fil: Ceballos, Tomás. Universidad de Valencia; España
Fil: Palma, Leopoldo. Universidad Publica de Navarra; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones y Transferencia de Villa María. Universidad Nacional de Villa María. Centro de Investigaciones y Transferencia de Villa María; Argentina
Fil: Escriche, Baltasar. Universidad de Valencia; España
Fil: Caballero, Primitivo. Universidad Publica de Navarra; España
Fil: Ferré, Juan. Universidad de Valencia; España
Materia
BIOINSECTICIDES
CROP PROTECTION
HISTOLOGICAL LOCALIZATION
INSECT PEST CONTROL
VEGETATIVE INSECTICIDAL PROTEINS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/97419

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal proteinGomis-Cebolla, JoaquínRuiz de Escudero, IñigoVera-Velasco, Natalia MaraHernández-Martínez, PatriciaHernández-Rodríguez, Carmen SaraCeballos, TomásPalma, LeopoldoEscriche, BaltasarCaballero, PrimitivoFerré, JuanBIOINSECTICIDESCROP PROTECTIONHISTOLOGICAL LOCALIZATIONINSECT PEST CONTROLVEGETATIVE INSECTICIDAL PROTEINShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately susceptible), Agrotis ipsilon and Ostrinia nubilalis (slightly susceptible). Processing Vip3Ca by O. nubilalis or M. brassicae midgut juice did not significantly changed its toxicity to either insect species, indicating that the low susceptibility of O. nubilalis is not due to a problem in the midgut processing of the toxin. M. brassicae larvae fed with Vip3Ca showed binding of this toxin to the apical membrane of the midgut epithelial cells. Histopathological inspection showed sloughing of the epithelial cells with further disruption, which suggests that the mode of action of Vip3Ca is similar to that described for Vip3Aa. Biotin-labeled Vip3Ca and Vip3Aa bound specifically to M. brassicae brush border membrane vesicles and both toxins competed for binding sites. This result suggests that insects resistant to Vip3A may also be cross-resistant to Vip3C, which has implications for Insect Resistance Management (IRM).Fil: Gomis-Cebolla, Joaquín. Universidad de Valencia; EspañaFil: Ruiz de Escudero, Iñigo. Universidad Publica de Navarra; EspañaFil: Vera-Velasco, Natalia Mara. Universidad de Valencia; EspañaFil: Hernández-Martínez, Patricia. Universidad de Valencia; EspañaFil: Hernández-Rodríguez, Carmen Sara. Universidad de Valencia; EspañaFil: Ceballos, Tomás. Universidad de Valencia; EspañaFil: Palma, Leopoldo. Universidad Publica de Navarra; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones y Transferencia de Villa María. Universidad Nacional de Villa María. Centro de Investigaciones y Transferencia de Villa María; ArgentinaFil: Escriche, Baltasar. Universidad de Valencia; EspañaFil: Caballero, Primitivo. Universidad Publica de Navarra; EspañaFil: Ferré, Juan. Universidad de Valencia; EspañaAcademic Press Inc Elsevier Science2017-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/97419Gomis-Cebolla, Joaquín; Ruiz de Escudero, Iñigo; Vera-Velasco, Natalia Mara; Hernández-Martínez, Patricia; Hernández-Rodríguez, Carmen Sara; et al.; Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein; Academic Press Inc Elsevier Science; Journal of Invertebrate Pathology; 142; 1-2017; 60-670022-2011CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022201116301550info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jip.2016.10.001info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:46:25Zoai:ri.conicet.gov.ar:11336/97419instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:46:26.152CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
title Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
spellingShingle Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
Gomis-Cebolla, Joaquín
BIOINSECTICIDES
CROP PROTECTION
HISTOLOGICAL LOCALIZATION
INSECT PEST CONTROL
VEGETATIVE INSECTICIDAL PROTEINS
title_short Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
title_full Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
title_fullStr Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
title_full_unstemmed Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
title_sort Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein
dc.creator.none.fl_str_mv Gomis-Cebolla, Joaquín
Ruiz de Escudero, Iñigo
Vera-Velasco, Natalia Mara
Hernández-Martínez, Patricia
Hernández-Rodríguez, Carmen Sara
Ceballos, Tomás
Palma, Leopoldo
Escriche, Baltasar
Caballero, Primitivo
Ferré, Juan
author Gomis-Cebolla, Joaquín
author_facet Gomis-Cebolla, Joaquín
Ruiz de Escudero, Iñigo
Vera-Velasco, Natalia Mara
Hernández-Martínez, Patricia
Hernández-Rodríguez, Carmen Sara
Ceballos, Tomás
Palma, Leopoldo
Escriche, Baltasar
Caballero, Primitivo
Ferré, Juan
author_role author
author2 Ruiz de Escudero, Iñigo
Vera-Velasco, Natalia Mara
Hernández-Martínez, Patricia
Hernández-Rodríguez, Carmen Sara
Ceballos, Tomás
Palma, Leopoldo
Escriche, Baltasar
Caballero, Primitivo
Ferré, Juan
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BIOINSECTICIDES
CROP PROTECTION
HISTOLOGICAL LOCALIZATION
INSECT PEST CONTROL
VEGETATIVE INSECTICIDAL PROTEINS
topic BIOINSECTICIDES
CROP PROTECTION
HISTOLOGICAL LOCALIZATION
INSECT PEST CONTROL
VEGETATIVE INSECTICIDAL PROTEINS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately susceptible), Agrotis ipsilon and Ostrinia nubilalis (slightly susceptible). Processing Vip3Ca by O. nubilalis or M. brassicae midgut juice did not significantly changed its toxicity to either insect species, indicating that the low susceptibility of O. nubilalis is not due to a problem in the midgut processing of the toxin. M. brassicae larvae fed with Vip3Ca showed binding of this toxin to the apical membrane of the midgut epithelial cells. Histopathological inspection showed sloughing of the epithelial cells with further disruption, which suggests that the mode of action of Vip3Ca is similar to that described for Vip3Aa. Biotin-labeled Vip3Ca and Vip3Aa bound specifically to M. brassicae brush border membrane vesicles and both toxins competed for binding sites. This result suggests that insects resistant to Vip3A may also be cross-resistant to Vip3C, which has implications for Insect Resistance Management (IRM).
Fil: Gomis-Cebolla, Joaquín. Universidad de Valencia; España
Fil: Ruiz de Escudero, Iñigo. Universidad Publica de Navarra; España
Fil: Vera-Velasco, Natalia Mara. Universidad de Valencia; España
Fil: Hernández-Martínez, Patricia. Universidad de Valencia; España
Fil: Hernández-Rodríguez, Carmen Sara. Universidad de Valencia; España
Fil: Ceballos, Tomás. Universidad de Valencia; España
Fil: Palma, Leopoldo. Universidad Publica de Navarra; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones y Transferencia de Villa María. Universidad Nacional de Villa María. Centro de Investigaciones y Transferencia de Villa María; Argentina
Fil: Escriche, Baltasar. Universidad de Valencia; España
Fil: Caballero, Primitivo. Universidad Publica de Navarra; España
Fil: Ferré, Juan. Universidad de Valencia; España
description The Vip3Ca protein, discovered in a screening of Spanish collections of Bacillus thuringiensis, was known to be toxic to Chrysodeixis chalcites, Mamestra brassicae and Trichoplusia ni. In the present study, its activity has been tested with additional insect species and we found that Cydia pomonella is moderately susceptible to this protein. Vip3Ca (of approximately 90 kDa) was processed to an approximately 70 kDa protein when incubated with midgut juice in all tested species. The kinetics of proteolysis correlated with the susceptibility of the insect species to Vip3Ca. The activation was faster to slower in the following order: M. brassicae (susceptible), Spodoptera littoralis (moderately susceptible), Agrotis ipsilon and Ostrinia nubilalis (slightly susceptible). Processing Vip3Ca by O. nubilalis or M. brassicae midgut juice did not significantly changed its toxicity to either insect species, indicating that the low susceptibility of O. nubilalis is not due to a problem in the midgut processing of the toxin. M. brassicae larvae fed with Vip3Ca showed binding of this toxin to the apical membrane of the midgut epithelial cells. Histopathological inspection showed sloughing of the epithelial cells with further disruption, which suggests that the mode of action of Vip3Ca is similar to that described for Vip3Aa. Biotin-labeled Vip3Ca and Vip3Aa bound specifically to M. brassicae brush border membrane vesicles and both toxins competed for binding sites. This result suggests that insects resistant to Vip3A may also be cross-resistant to Vip3C, which has implications for Insect Resistance Management (IRM).
publishDate 2017
dc.date.none.fl_str_mv 2017-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/97419
Gomis-Cebolla, Joaquín; Ruiz de Escudero, Iñigo; Vera-Velasco, Natalia Mara; Hernández-Martínez, Patricia; Hernández-Rodríguez, Carmen Sara; et al.; Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein; Academic Press Inc Elsevier Science; Journal of Invertebrate Pathology; 142; 1-2017; 60-67
0022-2011
CONICET Digital
CONICET
url http://hdl.handle.net/11336/97419
identifier_str_mv Gomis-Cebolla, Joaquín; Ruiz de Escudero, Iñigo; Vera-Velasco, Natalia Mara; Hernández-Martínez, Patricia; Hernández-Rodríguez, Carmen Sara; et al.; Insecticidal spectrum and mode of action of the Bacillus thuringiensis Vip3Ca insecticidal protein; Academic Press Inc Elsevier Science; Journal of Invertebrate Pathology; 142; 1-2017; 60-67
0022-2011
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0022201116301550
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jip.2016.10.001
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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