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Registro Completo |
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Biblioteca(s): |
Embrapa Milho e Sorgo; Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
08/10/2018 |
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Data da última atualização: |
24/11/2018 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SOUZA, C. S. F.; SILVEIRA, L. C. P.; PAULA, D. P.; ANDOW, D. A.; MENDES, S. M. |
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Afiliação: |
Camila S. F. Souza, Universidade Federal de Lavras; Luís C. P. Silveira, Universidade Federal de Lavras; DEBORA PIRES PAULA, Cenargen; David A. Andow, University of Minnesota; SIMONE MARTINS MENDES, CNPMS. |
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Título: |
Transfer of Cry1F from Bt maize to eggs of resistant Spodoptera frugiperda. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Plos One, v. 13, n. 9, e0203791, Sept. 2018. |
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DOI: |
10.1371 /journal.pone. 0203791 |
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Idioma: |
Inglês |
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Conteúdo: |
The intergenerational transfer of plant defense compounds by aposematic insects is well documented, and since 2006, has been shown for Cry toxins. Cry toxins are proteins naturally produced by the soil bacterium Bacillus thuringiensis (Bt) and its genes have been expressed in plants to confer insect pest resistance. In this work we tested if non-aposematic larvae of a major maize pest, Spodoptera frugiperda, with resistance to Cry1F, could transfer Cry1F from a genetically engineered maize variety to their offspring. Resistant 10day-old larvae that fed on Cry1F Bt maize until pupation were sexed and pair-mated to produce eggs. Using ELISA we found that Cry1F was transferred to offspring (1.47–4.42 ng Cry1F/10 eggs), a toxin concentration about 28–83 times less than that detected in Cry1F Bt maize leaves. This occurred when only one or both sexes were exposed, and more was transferred when both parents were exposed, with transitory detection in the first five egg masses. This work is an unprecedented demonstration that a non-aposematic, but resistant, species can transfer Cry1F to their offspring when exposed to Bt host plant leaves as immatures. |
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Palavras-Chave: |
Cry toxins; Lagarta-do-cartucho; Maize pest; Soil bacterium. |
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Thesagro: |
Bacillus Thuringiensis; Controle Biológico; Praga de Planta; Proteína. |
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Categoria do assunto: |
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H Saúde e Patologia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/186962/1/Transfer-Cry.pdf
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/184056/1/journal.pone.0203791.pdf
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Marc: |
LEADER 01964naa a2200277 a 4500
001 2099951
005 2018-11-24
008 2018 bl uuuu u00u1 u #d
024 7 $a10.1371 /journal.pone. 0203791$2DOI
100 1 $aSOUZA, C. S. F.
245 $aTransfer of Cry1F from Bt maize to eggs of resistant Spodoptera frugiperda.$h[electronic resource]
260 $c2018
520 $aThe intergenerational transfer of plant defense compounds by aposematic insects is well documented, and since 2006, has been shown for Cry toxins. Cry toxins are proteins naturally produced by the soil bacterium Bacillus thuringiensis (Bt) and its genes have been expressed in plants to confer insect pest resistance. In this work we tested if non-aposematic larvae of a major maize pest, Spodoptera frugiperda, with resistance to Cry1F, could transfer Cry1F from a genetically engineered maize variety to their offspring. Resistant 10day-old larvae that fed on Cry1F Bt maize until pupation were sexed and pair-mated to produce eggs. Using ELISA we found that Cry1F was transferred to offspring (1.47–4.42 ng Cry1F/10 eggs), a toxin concentration about 28–83 times less than that detected in Cry1F Bt maize leaves. This occurred when only one or both sexes were exposed, and more was transferred when both parents were exposed, with transitory detection in the first five egg masses. This work is an unprecedented demonstration that a non-aposematic, but resistant, species can transfer Cry1F to their offspring when exposed to Bt host plant leaves as immatures.
650 $aBacillus Thuringiensis
650 $aControle Biológico
650 $aPraga de Planta
650 $aProteína
653 $aCry toxins
653 $aLagarta-do-cartucho
653 $aMaize pest
653 $aSoil bacterium
700 1 $aSILVEIRA, L. C. P.
700 1 $aPAULA, D. P.
700 1 $aANDOW, D. A.
700 1 $aMENDES, S. M.
773 $tPlos One$gv. 13, n. 9, e0203791, Sept. 2018.
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Registro original: |
Embrapa Milho e Sorgo (CNPMS) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Suínos e Aves. Para informações adicionais entre em contato com cnpsa.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Suínos e Aves. |
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Data corrente: |
15/05/2018 |
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Data da última atualização: |
15/05/2018 |
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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: |
GAVA, D.; SERRÃO, V. H. B.; FERNANDES, L. T.; CANTAO, M. E.; ZANELLA, J. R. C.; MORES, N.; SCHAEFER, R. |
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Afiliação: |
DANIELLE GAVA, CNPSA; VITOR HUGO BALASCO SERRÃO, USP; LANA TEIXEIRA FERNANDES, CEDISA; MAURICIO EGIDIO CANTAO, CNPSA; JANICE REIS CIACCI ZANELLA, CNPSA; NELSON MORES, CNPSA; REJANE SCHAEFER, CNPSA. |
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Título: |
Structure analysis of capsid protein of porcine circovirus type 2 from pigs with systemic disease. |
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Ano de publicação: |
2018 |
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Fonte/Imprenta: |
Brazilian Journal of Microbiology, v. 49, p. 351-357, 2018. |
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DOI: |
10.1016/j.bjm.2017.08.007. |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: Economic losses with high mortality rate associated with Porcine circovirus type 2 (PCV2) is reported worldwide. PCV2 commercial vaccine was introduced in 2006 in U.S. and in 2008 in Brazil. Although PCV2 vaccines have been widely used, cases of PCV2 systemic disease have been reported in the last years. Eleven nursery or fattening pigs suffering from PCV2 systemic disease were selected from eight PCV2-vaccinated farms with historical records of PCV2 systemic disease in Southern Brazil. PCV2 genomes were amplified and sequenced from lymph node samples of selected pigs. The comparison among the ORF2 amino acid sequences of PCV2 isolates revealed three amino acid substitutions in the positions F57I, N178S and A190T, respectively. Using molecular modeling, a structural model for the capsid protein of PCV2 was built. Afterwards, the mutated residues positions were identified in the model. The structural analysis of the mutated residues showed that the external residue 190 is close to an important predicted region for antibodies recognition. Therefore, changes in the viral protein conformation might lead to an inefficient antibody binding and this could be a relevant mechanism underlying the recent vaccine failures observed in swine farms in Brazil Resumo: Perdas econômicas com alta taxa de mortalidade associada ao circovírus suíno tipo 2 (PCV2) são relatadas em todo o mundo. A vacina comercial PCV2 foi introduzida em 2006 nos EUA e em 2008 no Brasil. Embora as vacinas contra PCV2 tenham sido amplamente utilizadas, casos de doença sistêmica com PCV2 foram relatados nos últimos anos. Onze porcos de engorda ou engorda sofrendo de doença sistêmica de PCV2 foram selecionados de oito fazendas vacinadas com PCV2 com registros históricos de doença sistêmica de PCV2 no Sul do Brasil. Os genomas de PCV2 foram amplificados e sequenciados a partir de amostras de nodos linfáticos de porcos selecionados. A comparação entre as sequências de aminoácidos de ORF2 de isolados de PCV2 revelou três substituições de aminoácidos nas posições F57I, N178S e A190T, respectivamente. Usando modelagem molecular, um modelo estrutural para a proteína do capsídeo do PCV2 foi construído. Posteriormente, as posições dos resíduos mutados foram identificadas no modelo. A análise estrutural dos resíduos mutados mostrou que o resíduo externo 190 está próximo de uma importante região prevista para reconhecimento de anticorpos. Portanto, mudanças na conformação da proteína viral podem levar a uma ligação ineficiente do anticorpo, e isso poderia ser um mecanismo relevante subjacente às recentes falhas vacinais observadas em fazendas de suínos no Brasil. MenosAbstract: Economic losses with high mortality rate associated with Porcine circovirus type 2 (PCV2) is reported worldwide. PCV2 commercial vaccine was introduced in 2006 in U.S. and in 2008 in Brazil. Although PCV2 vaccines have been widely used, cases of PCV2 systemic disease have been reported in the last years. Eleven nursery or fattening pigs suffering from PCV2 systemic disease were selected from eight PCV2-vaccinated farms with historical records of PCV2 systemic disease in Southern Brazil. PCV2 genomes were amplified and sequenced from lymph node samples of selected pigs. The comparison among the ORF2 amino acid sequences of PCV2 isolates revealed three amino acid substitutions in the positions F57I, N178S and A190T, respectively. Using molecular modeling, a structural model for the capsid protein of PCV2 was built. Afterwards, the mutated residues positions were identified in the model. The structural analysis of the mutated residues showed that the external residue 190 is close to an important predicted region for antibodies recognition. Therefore, changes in the viral protein conformation might lead to an inefficient antibody binding and this could be a relevant mechanism underlying the recent vaccine failures observed in swine farms in Brazil Resumo: Perdas econômicas com alta taxa de mortalidade associada ao circovírus suíno tipo 2 (PCV2) são relatadas em todo o mundo. A vacina comercial PCV2 foi introduzida em 2006 nos EUA e em 2008 no Brasil. Embora as vacinas ... Mostrar Tudo |
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Palavras-Chave: |
Circovírus suíno tipo 2; PCV2. |
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Thesagro: |
Antígeno; Doença Animal; Imunização; Sanidade Animal; Virologia. |
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Thesaurus NAL: |
Animal diseases; Animal health; Antigenic variation; Capsid; Coat proteins; Epitopes; Molecular models; Porcine circovirus-2. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 03795naa a2200385 a 4500
001 2091466
005 2018-05-15
008 2018 bl uuuu u00u1 u #d
024 7 $a10.1016/j.bjm.2017.08.007.$2DOI
100 1 $aGAVA, D.
245 $aStructure analysis of capsid protein of porcine circovirus type 2 from pigs with systemic disease.$h[electronic resource]
260 $c2018
520 $aAbstract: Economic losses with high mortality rate associated with Porcine circovirus type 2 (PCV2) is reported worldwide. PCV2 commercial vaccine was introduced in 2006 in U.S. and in 2008 in Brazil. Although PCV2 vaccines have been widely used, cases of PCV2 systemic disease have been reported in the last years. Eleven nursery or fattening pigs suffering from PCV2 systemic disease were selected from eight PCV2-vaccinated farms with historical records of PCV2 systemic disease in Southern Brazil. PCV2 genomes were amplified and sequenced from lymph node samples of selected pigs. The comparison among the ORF2 amino acid sequences of PCV2 isolates revealed three amino acid substitutions in the positions F57I, N178S and A190T, respectively. Using molecular modeling, a structural model for the capsid protein of PCV2 was built. Afterwards, the mutated residues positions were identified in the model. The structural analysis of the mutated residues showed that the external residue 190 is close to an important predicted region for antibodies recognition. Therefore, changes in the viral protein conformation might lead to an inefficient antibody binding and this could be a relevant mechanism underlying the recent vaccine failures observed in swine farms in Brazil Resumo: Perdas econômicas com alta taxa de mortalidade associada ao circovírus suíno tipo 2 (PCV2) são relatadas em todo o mundo. A vacina comercial PCV2 foi introduzida em 2006 nos EUA e em 2008 no Brasil. Embora as vacinas contra PCV2 tenham sido amplamente utilizadas, casos de doença sistêmica com PCV2 foram relatados nos últimos anos. Onze porcos de engorda ou engorda sofrendo de doença sistêmica de PCV2 foram selecionados de oito fazendas vacinadas com PCV2 com registros históricos de doença sistêmica de PCV2 no Sul do Brasil. Os genomas de PCV2 foram amplificados e sequenciados a partir de amostras de nodos linfáticos de porcos selecionados. A comparação entre as sequências de aminoácidos de ORF2 de isolados de PCV2 revelou três substituições de aminoácidos nas posições F57I, N178S e A190T, respectivamente. Usando modelagem molecular, um modelo estrutural para a proteína do capsídeo do PCV2 foi construído. Posteriormente, as posições dos resíduos mutados foram identificadas no modelo. A análise estrutural dos resíduos mutados mostrou que o resíduo externo 190 está próximo de uma importante região prevista para reconhecimento de anticorpos. Portanto, mudanças na conformação da proteína viral podem levar a uma ligação ineficiente do anticorpo, e isso poderia ser um mecanismo relevante subjacente às recentes falhas vacinais observadas em fazendas de suínos no Brasil.
650 $aAnimal diseases
650 $aAnimal health
650 $aAntigenic variation
650 $aCapsid
650 $aCoat proteins
650 $aEpitopes
650 $aMolecular models
650 $aPorcine circovirus-2
650 $aAntígeno
650 $aDoença Animal
650 $aImunização
650 $aSanidade Animal
650 $aVirologia
653 $aCircovírus suíno tipo 2
653 $aPCV2
700 1 $aSERRÃO, V. H. B.
700 1 $aFERNANDES, L. T.
700 1 $aCANTAO, M. E.
700 1 $aZANELLA, J. R. C.
700 1 $aMORES, N.
700 1 $aSCHAEFER, R.
773 $tBrazilian Journal of Microbiology$gv. 49, p. 351-357, 2018.
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