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Registro Completo |
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Biblioteca(s): |
Embrapa Café. |
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Data corrente: |
16/03/2016 |
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Data da última atualização: |
21/03/2016 |
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Tipo da produção científica: |
Artigo em Anais de Congresso |
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Autoria: |
LIMA, E. A. de; CARNEIRO, F. de A.; RÊGO, E. C. S.; COSTA, T. S.; COTTA, M. G.; JORGE JÚNIOR, A.; MARRACCINI, P.; CARNEIRO, R. M. D. G.; ANDRADE, A. C. |
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Afiliação: |
EDRIANA ARAÚJO DE LIMA, Bolsista Consórcio Pesquisa Café; FERNANDA DE ARAÚJO CARNEIRO, Bolsista CAPES; ERICA CRISTINA SILVA RÊGO, Bolsista Consórcio Pesquisa Café; TATIANA SANTOS COSTA, UFLA; MICHEE GUITTON COTTA, Bolsista CAPES; ALDEMIRO JORGE JÚNIOR, Bolsista CAPES; PIERRE MARRACCINI, CIRAD/UMR/AGAP; REGINA MARIA DECHECHI GOMES CARNEIRO; ALAN CARVALHO ANDRADE, SAPC. |
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Título: |
Caracterização molecular e seleção de genes candidatos à resistência do clone 14 de Coffea canephora CONILON A Meloidogyne paranaensis. |
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Ano de publicação: |
2015 |
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Fonte/Imprenta: |
In: SIMPÓSIO DE PESQUISA DOS CAFÉS DO BRASIL, 9., 2015, Curitiba. Anais... Brasília, DF: Embrapa Café, 2015. |
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DOI: |
10.1002/rcm.7313 |
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Idioma: |
Português |
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Conteúdo: |
Os nematoides das galhas estão entre os patógenos mais nocivos para a agricultura cafeeira no Brasil e C. canephora tem se mostrado fonte de resistência a esses patógenos. Com o objetivo de identificar genes candidatos a resistência a M. paranaensis, dois clones de Coffea canephora Conilon previamente identificados como resistente (clone 14) e suscetível (clone 22), inoculados ou não em diferentes tempos com M. paranaensis, tiveram seus RNAs extraídos a partir das raizes, sequenciados, mapeados em genoma de referência de C. canephora e avaliados quantitativamente (expressão in silico) por meio de RNAseq e Excel. Dessa forma, foi possível identificar os genes que mais se expressaram no clone resistente em relação ao clone suscetível, e a respectiva expressão temporal foi relacionada à resistência a M. paranaensis. |
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Palavras-Chave: |
Candidates genes; Gene candidato Meloidogyne; RNAseq. |
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Thesagro: |
Coffea Canephora; Gene; Resistência. |
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Thesaurus Nal: |
Meloidogyne. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/141283/1/Caracterizacao-molecular-e-selecao.pdf
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Marc: |
LEADER 01827nam a2200301 a 4500
001 2041130
005 2016-03-21
008 2015 bl uuuu u00u1 u #d
024 7 $a10.1002/rcm.7313$2DOI
100 1 $aLIMA, E. A. de
245 $aCaracterização molecular e seleção de genes candidatos à resistência do clone 14 de Coffea canephora CONILON A Meloidogyne paranaensis.$h[electronic resource]
260 $aIn: SIMPÓSIO DE PESQUISA DOS CAFÉS DO BRASIL, 9., 2015, Curitiba. Anais... Brasília, DF: Embrapa Café$c2015
520 $aOs nematoides das galhas estão entre os patógenos mais nocivos para a agricultura cafeeira no Brasil e C. canephora tem se mostrado fonte de resistência a esses patógenos. Com o objetivo de identificar genes candidatos a resistência a M. paranaensis, dois clones de Coffea canephora Conilon previamente identificados como resistente (clone 14) e suscetível (clone 22), inoculados ou não em diferentes tempos com M. paranaensis, tiveram seus RNAs extraídos a partir das raizes, sequenciados, mapeados em genoma de referência de C. canephora e avaliados quantitativamente (expressão in silico) por meio de RNAseq e Excel. Dessa forma, foi possível identificar os genes que mais se expressaram no clone resistente em relação ao clone suscetível, e a respectiva expressão temporal foi relacionada à resistência a M. paranaensis.
650 $aMeloidogyne
650 $aCoffea Canephora
650 $aGene
650 $aResistência
653 $aCandidates genes
653 $aGene candidato Meloidogyne
653 $aRNAseq
700 1 $aCARNEIRO, F. de A.
700 1 $aRÊGO, E. C. S.
700 1 $aCOSTA, T. S.
700 1 $aCOTTA, M. G.
700 1 $aJORGE JÚNIOR, A.
700 1 $aMARRACCINI, P.
700 1 $aCARNEIRO, R. M. D. G.
700 1 $aANDRADE, A. C.
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Registro original: |
Embrapa Café (CNPCa) |
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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
001 2101792
005 2019-02-18
008 2018 bl uuuu u00u1 u #d
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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Embrapa Milho e Sorgo (CNPMS) |
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