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Registro Completo |
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Biblioteca(s): |
Embrapa Agrobiologia; Embrapa Agropecuária Oeste; Embrapa Amapá; Embrapa Amazônia Ocidental; Embrapa Amazônia Oriental; Embrapa Arroz e Feijão; Embrapa Meio Norte / UEP-Parnaíba; Embrapa Meio-Norte; Embrapa Rondônia; Embrapa Semiárido; Embrapa Unidades Centrais. MenosEmbrapa Agrobiologia; Embrapa Agropecuária Oeste; Embrapa Amapá; Embrapa Amazônia Ocidental; Embrapa Amazônia Oriental; Embrapa Arroz e Feijão; Embrapa Meio Norte / UEP-Parnaíba; Embrapa Meio-Norte; Embrapa Rondônia; Embrapa Semiárido... Mostrar Todas |
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Data corrente: |
20/05/2002 |
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Data da última atualização: |
09/05/2012 |
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Tipo da produção científica: |
Comunicado Técnico/Recomendações Técnicas |
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Autoria: |
BARRIGOSSI, J. A. F.; FERREIRA, E. |
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Afiliação: |
JOSE ALEXANDRE F BARRIGOSSI, CNPAF; EVANE FERREIRA, CNPAF. |
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Título: |
Tratamento de sementes de arroz com inseticidas: efeito sobre os insetos e rendimento de grãos. |
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Ano de publicação: |
2001 |
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Fonte/Imprenta: |
Santo Antônio de Goiás: Embrapa Arroz e Feijão, 2001. |
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Páginas: |
2 p. |
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Série: |
(Embrapa Arroz e Feijão. Pesquisa em foco, 59). |
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Idioma: |
Português |
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Conteúdo: |
Os insetos pragas de solo constituem uma preocupação permanente para os produtores de arroz de terras altas nos últimos anos agrícolas. Cupins e lagarta-elasmo são as principais pragas que atacam essa cultura na sua fase inicial. Os primeiros sinais de ataque da lagarta-elasmo ocorrem cerca de uma semana após a emergência das plantas. A folha central das plantas atacadas murcha, originando um sintoma conhecido como "coração-morto". Uma lagarta pode atacar várias plantas antes de completar seu ciclo biológico. Os cupins alimentam-se do sistema radicular das plantas. Para o controle, os produtores têm utilizado o tratamento de sementes com inseticidas, principalmente à base de carbofuran. Contudo, a eficiência desse produto, comparado a outros disponíveis atualmente no mercado, ainda não foi verificada em condições de campo. Além disso, a importância econômica do tratamento de sementes para os insetos pragas da cultura tem sido pouco avaliada.
Com este trabalho buscou-se determinar a eficiência de vários inseticidas aplicados às sementes no controle de insetos que atacam o arroz de terras altas na sua fase inicial.
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Palavras-Chave: |
Brasil; Controle; Goiás; Grain; Insect; Inseticidas; Insetos; Lagarta elasmo; Pest of plants; Rendimento de grãos; Santo Antônio de Goiás; Seed; Semente - Tratamento; Tratamento de sementes; Treatment. |
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Thesagro: |
Arroz; Cerrado; Controle Químico; Cupim; Entomologia; Grão; Inseticida; Inseto; Lagarta do Colo; Nasutitermes spp; Oryza Sativa; Praga; Praga de Planta; Semente; Tratamento; Tratamento de Semente. |
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Thesaurus Nal: |
chemical control; insecticides; rice; seeds. |
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Categoria do assunto: |
--
O Insetos e Entomologia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/59069/1/Foco-59.pdf
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Marc: |
LEADER 02605nam a2200565 a 4500
001 1209839
005 2012-05-09
008 2001 bl uuuu u0uu1 u #d
100 1 $aBARRIGOSSI, J. A. F.
245 $aTratamento de sementes de arroz com inseticidas$befeito sobre os insetos e rendimento de grãos.
260 $aSanto Antônio de Goiás: Embrapa Arroz e Feijão$c2001
300 $a2 p.
490 $a(Embrapa Arroz e Feijão. Pesquisa em foco, 59).
520 $aOs insetos pragas de solo constituem uma preocupação permanente para os produtores de arroz de terras altas nos últimos anos agrícolas. Cupins e lagarta-elasmo são as principais pragas que atacam essa cultura na sua fase inicial. Os primeiros sinais de ataque da lagarta-elasmo ocorrem cerca de uma semana após a emergência das plantas. A folha central das plantas atacadas murcha, originando um sintoma conhecido como "coração-morto". Uma lagarta pode atacar várias plantas antes de completar seu ciclo biológico. Os cupins alimentam-se do sistema radicular das plantas. Para o controle, os produtores têm utilizado o tratamento de sementes com inseticidas, principalmente à base de carbofuran. Contudo, a eficiência desse produto, comparado a outros disponíveis atualmente no mercado, ainda não foi verificada em condições de campo. Além disso, a importância econômica do tratamento de sementes para os insetos pragas da cultura tem sido pouco avaliada. Com este trabalho buscou-se determinar a eficiência de vários inseticidas aplicados às sementes no controle de insetos que atacam o arroz de terras altas na sua fase inicial.
650 $achemical control
650 $ainsecticides
650 $arice
650 $aseeds
650 $aArroz
650 $aCerrado
650 $aControle Químico
650 $aCupim
650 $aEntomologia
650 $aGrão
650 $aInseticida
650 $aInseto
650 $aLagarta do Colo
650 $aNasutitermes spp
650 $aOryza Sativa
650 $aPraga
650 $aPraga de Planta
650 $aSemente
650 $aTratamento
650 $aTratamento de Semente
653 $aBrasil
653 $aControle
653 $aGoiás
653 $aGrain
653 $aInsect
653 $aInseticidas
653 $aInsetos
653 $aLagarta elasmo
653 $aPest of plants
653 $aRendimento de grãos
653 $aSanto Antônio de Goiás
653 $aSeed
653 $aSemente - Tratamento
653 $aTratamento de sementes
653 $aTreatment
700 1 $aFERREIRA, E.
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Registro original: |
Embrapa Arroz e Feijão (CNPAF) |
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Voltar
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital; Embrapa Meio Ambiente. |
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Data corrente: |
20/04/2006 |
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Data da última atualização: |
31/08/2015 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
JESUS, K. R. E. de; FALCAO, P. R. K.; NESHICH, G. |
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Afiliação: |
KATIA REGINA EVARISTO DE JESUS, CNPMA; PAULA REGINA KUSER FALCAO, CNPTIA; GORAN NESHICH, CNPTIA. |
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Título: |
Structural analyses of CRY 1Ac protein from Bacillus thuringiensis. |
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Ano de publicação: |
2005 |
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Fonte/Imprenta: |
In: X-MEETING INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu/MG. Presented posters. Caxambu/MG: Associação Brasileira de Bioinformática e Biologia Computacional, 2005. p. 133. |
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Idioma: |
Inglês
Português |
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Conteúdo: |
Cry protein is a delta endotoxin of the Bacillus family that provides an entomopatogenic activity to Bacilius thuringiensis. These proteins have a specific toxic activity against three types of insect larva: Lepdopthera, Diptera and Coleopthera. The insecticidal toxins are produced during spore formation. When an insect ingests these proteins they are activated by proteolytic cleavage. The toxin, after the ingestion, is solubitized by the alcalin pH in the digestive tract of the target insect. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. These proteins are the active agents used in the majority of biorational pesticides and insect-resistant transgenic crops. This activated region of the delta endotoxin is composed of three structural domains. Domain I is involved in membrane insertion, pore formation and toxicity. The second and third domains are involved in receptor binding and specifically domain III is important in insect specificity. There are around 120 sequences of Cry toxins, and only five structures were deposited on the Protein Data Bank (PDB). There is a large interest in the toxin Cry 1Ac because it is commonly used to create transgenic plants with insect resistance. A theoretical model of the Cry lAc toxin was obtained on the basis of the coordinates of the insecticidal protein Cry lAa (PDB code:lciy.pdb) [1] as a template. The high sequence identity (73%) and a good correlation coefficient obtained from the elctron density server [2] indicates that 1ciy structure could be used as a template. The model corresponds to residues 33-618 of the primary structure and consists of domains I, II and III. The sequence of domain I is highly conserved, while domain II and III have the lower sequence similarity. The 3D model was construct using Modeller v7.7 [3]. Aimed at verifying whether the amino acid differences in domains II and III could be responsible for insect specifícity, this two structures were structurally aligned and compared with the Sting protein structure analysis program. Knowing that each amino acid substitution could potentially affect the protein structure and function, these amino acids were mapped and evaluated according to: conservation, change in solvent accessibility, side-chain volume change, effect on amino-acid interactions, protein electrostatics, and physicochemical properties of amino acids. Such approach can open a new insight into understanding of specificity that Cry protein has for receptors in plant pests and can help in the design of mutagenesis experiments aimed to elucidate the mechanism of action of the CrylAc toxin. MenosCry protein is a delta endotoxin of the Bacillus family that provides an entomopatogenic activity to Bacilius thuringiensis. These proteins have a specific toxic activity against three types of insect larva: Lepdopthera, Diptera and Coleopthera. The insecticidal toxins are produced during spore formation. When an insect ingests these proteins they are activated by proteolytic cleavage. The toxin, after the ingestion, is solubitized by the alcalin pH in the digestive tract of the target insect. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. These proteins are the active agents used in the majority of biorational pesticides and insect-resistant transgenic crops. This activated region of the delta endotoxin is composed of three structural domains. Domain I is involved in membrane insertion, pore formation and toxicity. The second and third domains are involved in receptor binding and specifically domain III is important in insect specificity. There are around 120 sequences of Cry toxins, and only five structures were deposited on the Protein Data Bank (PDB). There is a large interest in the toxin Cry 1Ac because it is commonly used to create transgenic plants with insect resistance. A theoretical model of the Cry lAc toxin was obtained on the basis of the coordinates of the insecticidal protein Cry lAa (PDB code:lciy.pdb) [1] as a template. The high sequence identity (73%) and a good correlation coefficient obtained from the elc... Mostrar Tudo |
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Palavras-Chave: |
Bioinformática. |
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Thesagro: |
Bacillus thuringiensis; Proteina. |
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Thesaurus NAL: |
Bioinformatics; Proteins. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/127545/1/2005RA-078.pdf
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Marc: |
LEADER 03359nam a2200193 a 4500
001 2021515
005 2015-08-31
008 2005 bl uuuu u00u1 u #d
100 1 $aJESUS, K. R. E. de
245 $aStructural analyses of CRY 1Ac protein from Bacillus thuringiensis.$h[electronic resource]
260 $aIn: X-MEETING INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu/MG. Presented posters. Caxambu/MG: Associação Brasileira de Bioinformática e Biologia Computacional, 2005. p. 133.$c2005
520 $aCry protein is a delta endotoxin of the Bacillus family that provides an entomopatogenic activity to Bacilius thuringiensis. These proteins have a specific toxic activity against three types of insect larva: Lepdopthera, Diptera and Coleopthera. The insecticidal toxins are produced during spore formation. When an insect ingests these proteins they are activated by proteolytic cleavage. The toxin, after the ingestion, is solubitized by the alcalin pH in the digestive tract of the target insect. Once activated the endotoxin binds to the gut epithelium and causes cell lysis leading to death. These proteins are the active agents used in the majority of biorational pesticides and insect-resistant transgenic crops. This activated region of the delta endotoxin is composed of three structural domains. Domain I is involved in membrane insertion, pore formation and toxicity. The second and third domains are involved in receptor binding and specifically domain III is important in insect specificity. There are around 120 sequences of Cry toxins, and only five structures were deposited on the Protein Data Bank (PDB). There is a large interest in the toxin Cry 1Ac because it is commonly used to create transgenic plants with insect resistance. A theoretical model of the Cry lAc toxin was obtained on the basis of the coordinates of the insecticidal protein Cry lAa (PDB code:lciy.pdb) [1] as a template. The high sequence identity (73%) and a good correlation coefficient obtained from the elctron density server [2] indicates that 1ciy structure could be used as a template. The model corresponds to residues 33-618 of the primary structure and consists of domains I, II and III. The sequence of domain I is highly conserved, while domain II and III have the lower sequence similarity. The 3D model was construct using Modeller v7.7 [3]. Aimed at verifying whether the amino acid differences in domains II and III could be responsible for insect specifícity, this two structures were structurally aligned and compared with the Sting protein structure analysis program. Knowing that each amino acid substitution could potentially affect the protein structure and function, these amino acids were mapped and evaluated according to: conservation, change in solvent accessibility, side-chain volume change, effect on amino-acid interactions, protein electrostatics, and physicochemical properties of amino acids. Such approach can open a new insight into understanding of specificity that Cry protein has for receptors in plant pests and can help in the design of mutagenesis experiments aimed to elucidate the mechanism of action of the CrylAc toxin.
650 $aBioinformatics
650 $aProteins
650 $aBacillus thuringiensis
650 $aProteina
653 $aBioinformática
700 1 $aFALCAO, P. R. K.
700 1 $aNESHICH, G.
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Registro original: |
Embrapa Meio Ambiente (CNPMA) |
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