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| Registros recuperados : 13 | |
| 4. |  | QUEIROZ, P. R.; RAMIRO, C. A.; MARTINS, E. S.; SOBERÓN, M.; BRAVO, A.; PONTES, R. G. M. S. de. Mitochondrial markers to distinguish Spodoptera frugiperda populations associated with corn and cotton crops. Pesquisa Agropecuária Brasileira, Brasília, DF v. 51, n. 5, p.692-696, maio, 2016. Notas científicas.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia; Embrapa Unidades Centrais. |
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| 5. | | MARTINS, E.; MACEDO, C.; QUEIROZ, P.; PRACA, L.; SOARES, C. M.; MOREIRA, H.; GRISI, I.; SOBERON, M.; BRAVO, A.; MONNERAT, R. Resistência de Spodoptera frugiperda em cultivo de milho Cry1F. In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 25., 2014, Goiânia. Entomologia integrada à sociedade para o desenvolvimento sustentável: anais. Goiânia: Sociedade Entomológica do Brasil, 2014. Resumo 1571.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 6. | | SILVA, I. H. S. da; GOMÉZ, I.; SÁNCHEZ, J.; CASTRO, D. L. M. de; VALICENTE, F. H.; SOBERÓN, M.; POLANCZYK, R. A.; BRAVO, A. Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin. Plos One, San Francisco, v. 13, n. 12, e0207789, 2018.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 7. | | SILVA, I. H. S.; GOMEZ, I.; SANCHEZ, J.; CASTRO, D. L. M.; VALICENTE, F. H.; SOBERON, M.; POLANCZYK, R. A.; BRAVO, A. Identification of midgut membrane proteins from different instars of Helicoverpa armigera that bind to Cry1Ac toxin. In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 27.; CONGRESSO LATINO-AMERICANO DE ENTOMOLOGIA, 10., 2018, Gramado. Saúde, ambiente e agricultura: anais. Gramado: SEB, 2018. p. 1348.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 8. | | SILVA, I. H. S.; NASCIMENTO, J. do; SANCHES, A. C.; DESIDERIO, J. A.; VALICENTE, F. H.; SOBERON, M.; POLANCZYK, R. A.; BRAVO, A. Degradation of Cry1Ac protoxin can explain the decreased susceptibility in late instars of Helicoverpa armigera. In: CONGRESSO BRASILEIRO DE ENTOMOLOGIA, 27.; CONGRESSO LATINO-AMERICANO DE ENTOMOLOGIA, 10., 2018, Gramado. Saúde, ambiente e agricultura: anais. Gramado: SEB, 2018. p. 1341.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 9. | | MONNERAT, R.; MARTINS, E.; MACEDO, C.; QUEIROZ, P.; PRAÇA, L.; SOARES, C. M.; MOREIRA, H.; GRISI, I.; SILVA, J.; SOBERON, M.; BRAVO, A. Evidence of field-evolved resistance of Spodoptera frugiperda to Bt corn expressing Cry1F in Brazil that is still sensitive to modified bt toxins. PLoS One, v. 10, Apr 2015. (Open Access).| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 10. | | MONNERAT, R.; PEREIRA, E.; TELES, B.; MARTINS, E.; PRACA, L.; QUEIROZ, P.; SOBERON, M.; BRAVO, A.; RAMOS, F.; SOARES, C. M. Synergistic activity of Bacillus thuringiensis toxins against Simulium spp. larvae. Journal of Invertebrate Pathology, v .121, p.70-73, 2014.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 11. | | GÓMEZ, I.; SÁNCHEZ, J.; LIMA, C.; MARTINS, E.; ROSALES-JUÁREZ, A.; AGUILAR-MEDEL, S.; ABAD, A.; DONG, H.; PONTES, R. G. M. S. de; PEÑA, G.; ZHANG, J.; NELSON, M.; WU, G.; BRAVO, A.; SOBERÓN, M. Enhancement of Bacillus thuringiensis Cry1Ab and Cry1Fa toxicity to Spodoptera frugiperda by domain III mutations indicates there are two limiting steps in toxicity as defined by receptor binding and protein stability Applied and Environmental Microbiology, v. 84, n. 20, article e01393-18, 2018. Na publicação: Rose Monnerat.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 12. | | MONNERAT, R.; MARTINS, E.; QUEIROZ, P.; ORDÚZ, S.; JARAMILLO, G.; BENINTENDE, G.; COZZI, J.; REAL, M. D.; MARTINEZ-RAMIREZ, A.; RAUSELL, C.; CERÓN, J.; IBARRA, J. E.; RINCON-CASTRO, M. C. del; ESPINOZA, A. M.; MEZA-BASSO, L.; CABRERA, L.; SÁNCHEZ, J.; SOBERON, M.; BRAVO, A. Genetic variability of Spodoptera frugiperda Smith (Lepidoptera: Noctuidae) populations from Latin America is associated with variations in susceptibility to Bacillus thuringiensis cry toxins. Applied and Environmental Microbiology, v. 72, n. 11, p. 7029-7035, 2006.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 13. | | MARTINS, E. S.; MONNERAT, R. G.; QUEIROZ, P. R.; ORDUZ, S.; BENINTENDE, G.; COZZI, J.; REAL, M. D.; MARTINEZ-RAMIREZ, A.; RAUSELL, C.; CERÓN, J.; IBARRA, J. E.; RINCON-CASTRO, M. C. D.; ESPINOZA, A. M.; MEZA-BASSO, L.; CABRERA, L.; SÁNCHEZ, J.; SOBERON, M.; BRAVO, A. A variabilidade genética em populações de Spodoptera frugiperda Smith (Lepidoptera: Noctuidae) da América Latina está associada a variações de suceptibilidade a toxinas Cry de Bacillus thuringiensis. In: ENCONTRO DO TALENTO ESTUDANTIL DA EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA, 11., 2006, Brasília, DF. Anais: resumos dos trabalhos. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2006. p. 122.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| Registros recuperados : 13 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
17/12/2018 |
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Data da última atualização: |
18/02/2019 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
SILVA, I. H. S. da; GOMÉZ, I.; SÁNCHEZ, J.; CASTRO, D. L. M. de; VALICENTE, F. H.; SOBERÓN, M.; POLANCZYK, R. A.; BRAVO, A. |
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Afiliação: |
Igor Henrique Sena da Silva, Universidade Estadual Paulista; Isabel Goméz, Universidad Nacional Autónoma de México; Jorge Sánchez, Universidad Nacional Autónoma de México; Diana L. Martínez de Castro, Universidad Nacional Autónoma de México; FERNANDO HERCOS VALICENTE, CNPMS; Mario Soberón, Universidad Nacional Autónoma de México; Ricardo Antonio Polanczyk, Universidade Estadual Paulista; Alejandra Bravo, Universidad Nacional Autónoma de México. |
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Título: |
Identification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera: Noctuidae) that bind to Cry1Ac toxin. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Plos One, San Francisco, v. 13, n. 12, e0207789, 2018. |
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DOI: |
10.1371/journal.pone.0207789 |
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Idioma: |
Inglês |
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Conteúdo: |
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. MenosHelicoverpa 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, suggesti... Mostrar Tudo |
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Thesagro: |
Praga de Planta; Proteína; Toxina. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/188667/1/Identification-midgut.pdf
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Marc: |
LEADER 02401naa a2200253 a 4500
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024 7 $a10.1371/journal.pone.0207789$2DOI
100 1 $aSILVA, I. H. S. da
245 $aIdentification of midgut membrane proteins from different instars of Helicoverpa armigera (Lepidoptera$bNoctuidae) that bind to Cry1Ac toxin.$h[electronic resource]
260 $c2018
520 $aHelicoverpa 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.
650 $aPraga de Planta
650 $aProteína
650 $aToxina
700 1 $aGOMÉZ, I.
700 1 $aSÁNCHEZ, J.
700 1 $aCASTRO, D. L. M. de
700 1 $aVALICENTE, F. H.
700 1 $aSOBERÓN, M.
700 1 $aPOLANCZYK, R. A.
700 1 $aBRAVO, A.
773 $tPlos One, San Francisco$gv. 13, n. 12, e0207789, 2018.
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