Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds

Detalhes bibliográficos
Autor(a) principal: Gomes, Angelica de Paula Galvão
Data de Publicação: 2005
Outros Autores: Dias, Simoni Campos, Bloch Junior, Carlos, Melo, Francislete Rodrigues, Furtado Junior, José de Ribamar, Pontes, Rose Gomes Monnerat Solon de, Sá, Maria Fatima Grossi de, Franco, Octávio Luiz
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UCB
Texto Completo: http://twingo.ucb.br:8080/jspui/handle/10869/597
https://repositorio.ucb.br:9443/jspui/handle/123456789/7766
Resumo: Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil.
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spelling Gomes, Angelica de Paula GalvãoDias, Simoni CamposBloch Junior, CarlosMelo, Francislete RodriguesFurtado Junior, José de RibamarPontes, Rose Gomes Monnerat Solon deSá, Maria Fatima Grossi deFranco, Octávio Luiz2016-10-10T03:52:36Z2016-10-10T03:52:36Z2005GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005.10964959http://twingo.ucb.br:8080/jspui/handle/10869/597https://repositorio.ucb.br:9443/jspui/handle/123456789/7766Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil.Made available in DSpace on 2016-10-10T03:52:36Z (GMT). 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dc.title.pt_BR.fl_str_mv Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
title Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
spellingShingle Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
Gomes, Angelica de Paula Galvão
Serine proteinase inhibitor
Cicer arietinum
Anthonomus grandis
Plant defense
Cotton
Mass spectrometry
Trypsin
Digestive enzymes
title_short Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
title_full Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
title_fullStr Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
title_full_unstemmed Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
title_sort Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
author Gomes, Angelica de Paula Galvão
author_facet Gomes, Angelica de Paula Galvão
Dias, Simoni Campos
Bloch Junior, Carlos
Melo, Francislete Rodrigues
Furtado Junior, José de Ribamar
Pontes, Rose Gomes Monnerat Solon de
Sá, Maria Fatima Grossi de
Franco, Octávio Luiz
author_role author
author2 Dias, Simoni Campos
Bloch Junior, Carlos
Melo, Francislete Rodrigues
Furtado Junior, José de Ribamar
Pontes, Rose Gomes Monnerat Solon de
Sá, Maria Fatima Grossi de
Franco, Octávio Luiz
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Gomes, Angelica de Paula Galvão
Dias, Simoni Campos
Bloch Junior, Carlos
Melo, Francislete Rodrigues
Furtado Junior, José de Ribamar
Pontes, Rose Gomes Monnerat Solon de
Sá, Maria Fatima Grossi de
Franco, Octávio Luiz
dc.subject.por.fl_str_mv Serine proteinase inhibitor
Cicer arietinum
Anthonomus grandis
Plant defense
Cotton
Mass spectrometry
Trypsin
Digestive enzymes
topic Serine proteinase inhibitor
Cicer arietinum
Anthonomus grandis
Plant defense
Cotton
Mass spectrometry
Trypsin
Digestive enzymes
dc.description.abstract.por.fl_txt_mv Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil.
dc.description.version.pt_BR.fl_txt_mv Sim
dc.description.status.pt_BR.fl_txt_mv Publicado
description Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil.
publishDate 2005
dc.date.issued.fl_str_mv 2005
dc.date.accessioned.fl_str_mv 2016-10-10T03:52:36Z
dc.date.available.fl_str_mv 2016-10-10T03:52:36Z
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dc.identifier.citation.fl_str_mv GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005.
dc.identifier.uri.fl_str_mv http://twingo.ucb.br:8080/jspui/handle/10869/597
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identifier_str_mv GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005.
10964959
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