Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1371/journal.pone.0207789 http://hdl.handle.net/11449/185178 |
Resumo: | Helicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesting that increased proteolytic activity on the toxin could also explain the low Cry1Ac toxicity in late instars. |
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Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxinHelicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesting that increased proteolytic activity on the toxin could also explain the low Cry1Ac toxicity in late instars.Direccion General de Asuntos del personal Academico DGAPAFronteras de la CienciaConsejo Nacional de Ciencia y Tecnologia CONACyTFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)DGAPACONACyT Fronteras de la CienciaUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Fitossanidade, Jaboticabal, SP, BrazilUniv Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca, Morelos, MexicoEmbrapa Milho & Sorgo, Sete Lagoas, MG, BrazilUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Fitossanidade, Jaboticabal, SP, BrazilDireccion General de Asuntos del personal Academico DGAPA: IN201016Fronteras de la Ciencia: 008Consejo Nacional de Ciencia y Tecnologia CONACyT: 2015/24330-5Consejo Nacional de Ciencia y Tecnologia CONACyT: 2016/21464-3DGAPA: IN201016CONACyT Fronteras de la Ciencia: 008FAPESP: 2015/24330-5FAPESP: 2016/21464-3Public Library ScienceUniversidade Estadual Paulista (Unesp)Univ Nacl Autonoma MexicoEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)Sena Da Silva, Igor Henrique [UNESP]Gomez, IsabelSanchez, JorgeMartinez de Castro, Diana L.Valicente, Fernando HercosSoberon, MarioPolanczyk, Ricardo Antonio [UNESP]Bravo, Alejandra2019-10-04T12:33:12Z2019-10-04T12:33:12Z2018-12-06info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article16http://dx.doi.org/10.1371/journal.pone.0207789Plos One. San Francisco: Public Library Science, v. 13, n. 12, 16 p., 2018.1932-6203http://hdl.handle.net/11449/18517810.1371/journal.pone.0207789WOS:00045230760001927881567925328700000-0003-0769-9902Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPlos Oneinfo:eu-repo/semantics/openAccess2021-10-22T22:17:24Zoai:repositorio.unesp.br:11449/185178Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-22T22:17:24Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
title |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
spellingShingle |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin Sena Da Silva, Igor Henrique [UNESP] |
title_short |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
title_full |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
title_fullStr |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
title_full_unstemmed |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
title_sort |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin |
author |
Sena Da Silva, Igor Henrique [UNESP] |
author_facet |
Sena Da Silva, Igor Henrique [UNESP] Gomez, Isabel Sanchez, Jorge Martinez de Castro, Diana L. Valicente, Fernando Hercos Soberon, Mario Polanczyk, Ricardo Antonio [UNESP] Bravo, Alejandra |
author_role |
author |
author2 |
Gomez, Isabel Sanchez, Jorge Martinez de Castro, Diana L. Valicente, Fernando Hercos Soberon, Mario Polanczyk, Ricardo Antonio [UNESP] Bravo, Alejandra |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Univ Nacl Autonoma Mexico Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA) |
dc.contributor.author.fl_str_mv |
Sena Da Silva, Igor Henrique [UNESP] Gomez, Isabel Sanchez, Jorge Martinez de Castro, Diana L. Valicente, Fernando Hercos Soberon, Mario Polanczyk, Ricardo Antonio [UNESP] Bravo, Alejandra |
description |
Helicoverpa armigera is a polyphagous pest sensitive to Cry1Ac protein from Bacillus thuringiensis (Bt). The susceptibility of the different larval instars of H. armigera to Cry1Ac protoxin showed a significant 45-fold reduction in late instars compared to early instars. A possible hypothesis is that gut surface proteins that bind to Cry1Ac differ in both instars, although higher Cry toxin degradation in late instars could also explain the observed differences in susceptibility. Here we compared the Cry1Ac-binding proteins from second and fifth instars by pull-down assays and liquid chromatography coupled to mass spectrometry analysis (LC-MS/MS). The data show differential protein interaction patterns of Cry1Ac in the two instars analyzed. Alkaline phosphatase, and other membrane proteins, such as prohibitin and an anion selective channel protein were identified only in the second instar, suggesting that these proteins may be involved in the higher toxicity of Cry1Ac in early instars of H. armigera. Eleven Cry1Ac binindg proteins were identified exclusively in late instar larvae, like different proteases such as trypsin-like protease, azurocidin-like proteinase, and carboxypeptidase. Different aminopeptidase N isofroms were identified in both instar larvae. We compared the Cry1Ac protoxin degradation using midgut juice from late and early instars, showing that the midgut juice from late instars is more efficient to degrade Cry1Ac protoxin than that of early instars, suggesting that increased proteolytic activity on the toxin could also explain the low Cry1Ac toxicity in late instars. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-06 2019-10-04T12:33:12Z 2019-10-04T12:33:12Z |
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/10.1371/journal.pone.0207789 Plos One. San Francisco: Public Library Science, v. 13, n. 12, 16 p., 2018. 1932-6203 http://hdl.handle.net/11449/185178 10.1371/journal.pone.0207789 WOS:000452307600019 2788156792532870 0000-0003-0769-9902 |
url |
http://dx.doi.org/10.1371/journal.pone.0207789 http://hdl.handle.net/11449/185178 |
identifier_str_mv |
Plos One. San Francisco: Public Library Science, v. 13, n. 12, 16 p., 2018. 1932-6203 10.1371/journal.pone.0207789 WOS:000452307600019 2788156792532870 0000-0003-0769-9902 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Plos One |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
16 |
dc.publisher.none.fl_str_mv |
Public Library Science |
publisher.none.fl_str_mv |
Public Library Science |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
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UNESP |
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UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1792962089581543424 |