First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds

Detalhes bibliográficos
Autor(a) principal: Almeida Filho, Luiz C. P.
Data de Publicação: 2018
Outros Autores: Tabosa, Pedro Matheus Sousa, Hissa, Denise Cavalcante, Vasconcelos, Ilka M., Carvalho, Ana F. U.
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/62916
Resumo: BACKGROUND: Arboviroses such as dengue, Zika and chikungunya represent a serious public health issue as a consequenceof the absence of approved vaccines or specific antiviral drugs against the arboviruses that cause them. One way to preventthese diseases is by combating the vector mosquito, Aedes aegypti (Diptera), which has serine proteases in the midgut. Proteaseinhibitors are molecules that can block enzyme activity, impairing digestion and nutrition, which can lead to death. Thus, wepurified and characterized a novel chymotrypsin-trypsin inhibitor (LsCTI) from Lonchocarpus sericeus seeds and investigated itseffect upon Ae. aegypti egg hatching, larval development and digestive proteases.RESULTS: LsCTI showed a single protein band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE),and the molecular mass determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry(MALDI-TOF-MS) was 8870.45 Da. Kinetics analyses revealed a noncompetitive type of inhibition and low inhibition con-stant (Ki) for chymotrypsin (8.24 x 10-8M). The thermal resistance was remarkable, even at 100∘C for 180 min. The inhibitorconcentration required for 50-percent enzyme inhibition (IC50) of LsCTI was 4.7 x 10-7M for Ae. aegypti midgut larval enzymes.LsCTI did not affect egg hatchability at 0.3 mg mL-1, but caused a high larval mortality rate (77%) and delayed development(37%).CONCLUSIONS: LsCTI is a novel protease inhibitor with remarkable biochemical characteristics and is a potential tool to controlAe. aegypti development.© 2017 Society of Chemical Industry
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spelling First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seedsChymotrypsin inhibitorLonchocarpusLegume seedsDengueMidgut enzymesZikaBACKGROUND: Arboviroses such as dengue, Zika and chikungunya represent a serious public health issue as a consequenceof the absence of approved vaccines or specific antiviral drugs against the arboviruses that cause them. One way to preventthese diseases is by combating the vector mosquito, Aedes aegypti (Diptera), which has serine proteases in the midgut. Proteaseinhibitors are molecules that can block enzyme activity, impairing digestion and nutrition, which can lead to death. Thus, wepurified and characterized a novel chymotrypsin-trypsin inhibitor (LsCTI) from Lonchocarpus sericeus seeds and investigated itseffect upon Ae. aegypti egg hatching, larval development and digestive proteases.RESULTS: LsCTI showed a single protein band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE),and the molecular mass determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry(MALDI-TOF-MS) was 8870.45 Da. Kinetics analyses revealed a noncompetitive type of inhibition and low inhibition con-stant (Ki) for chymotrypsin (8.24 x 10-8M). The thermal resistance was remarkable, even at 100∘C for 180 min. The inhibitorconcentration required for 50-percent enzyme inhibition (IC50) of LsCTI was 4.7 x 10-7M for Ae. aegypti midgut larval enzymes.LsCTI did not affect egg hatchability at 0.3 mg mL-1, but caused a high larval mortality rate (77%) and delayed development(37%).CONCLUSIONS: LsCTI is a novel protease inhibitor with remarkable biochemical characteristics and is a potential tool to controlAe. aegypti development.© 2017 Society of Chemical IndustryPest Manag Sci2021-12-10T17:06:11Z2021-12-10T17:06:11Z2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfALMEIDA FILHO, Luiz C. P. et al. First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds. Pest Manag Sci, [s. l.], v. 74, n. 6, p. 1362-1373, 2018.http://www.repositorio.ufc.br/handle/riufc/62916Almeida Filho, Luiz C. P.Tabosa, Pedro Matheus SousaHissa, Denise CavalcanteVasconcelos, Ilka M.Carvalho, Ana F. U.info:eu-repo/semantics/openAccessporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFC2023-10-10T19:34:09Zoai:repositorio.ufc.br:riufc/62916Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:29:19.456591Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
title First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
spellingShingle First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
Almeida Filho, Luiz C. P.
Chymotrypsin inhibitor
Lonchocarpus
Legume seeds
Dengue
Midgut enzymes
Zika
title_short First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
title_full First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
title_fullStr First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
title_full_unstemmed First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
title_sort First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds
author Almeida Filho, Luiz C. P.
author_facet Almeida Filho, Luiz C. P.
Tabosa, Pedro Matheus Sousa
Hissa, Denise Cavalcante
Vasconcelos, Ilka M.
Carvalho, Ana F. U.
author_role author
author2 Tabosa, Pedro Matheus Sousa
Hissa, Denise Cavalcante
Vasconcelos, Ilka M.
Carvalho, Ana F. U.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Almeida Filho, Luiz C. P.
Tabosa, Pedro Matheus Sousa
Hissa, Denise Cavalcante
Vasconcelos, Ilka M.
Carvalho, Ana F. U.
dc.subject.por.fl_str_mv Chymotrypsin inhibitor
Lonchocarpus
Legume seeds
Dengue
Midgut enzymes
Zika
topic Chymotrypsin inhibitor
Lonchocarpus
Legume seeds
Dengue
Midgut enzymes
Zika
description BACKGROUND: Arboviroses such as dengue, Zika and chikungunya represent a serious public health issue as a consequenceof the absence of approved vaccines or specific antiviral drugs against the arboviruses that cause them. One way to preventthese diseases is by combating the vector mosquito, Aedes aegypti (Diptera), which has serine proteases in the midgut. Proteaseinhibitors are molecules that can block enzyme activity, impairing digestion and nutrition, which can lead to death. Thus, wepurified and characterized a novel chymotrypsin-trypsin inhibitor (LsCTI) from Lonchocarpus sericeus seeds and investigated itseffect upon Ae. aegypti egg hatching, larval development and digestive proteases.RESULTS: LsCTI showed a single protein band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE),and the molecular mass determined by matrix-assisted laser desorption ionization time-of-flight mass spectrometry(MALDI-TOF-MS) was 8870.45 Da. Kinetics analyses revealed a noncompetitive type of inhibition and low inhibition con-stant (Ki) for chymotrypsin (8.24 x 10-8M). The thermal resistance was remarkable, even at 100∘C for 180 min. The inhibitorconcentration required for 50-percent enzyme inhibition (IC50) of LsCTI was 4.7 x 10-7M for Ae. aegypti midgut larval enzymes.LsCTI did not affect egg hatchability at 0.3 mg mL-1, but caused a high larval mortality rate (77%) and delayed development(37%).CONCLUSIONS: LsCTI is a novel protease inhibitor with remarkable biochemical characteristics and is a potential tool to controlAe. aegypti development.© 2017 Society of Chemical Industry
publishDate 2018
dc.date.none.fl_str_mv 2018
2021-12-10T17:06:11Z
2021-12-10T17:06:11Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv ALMEIDA FILHO, Luiz C. P. et al. First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds. Pest Manag Sci, [s. l.], v. 74, n. 6, p. 1362-1373, 2018.
http://www.repositorio.ufc.br/handle/riufc/62916
identifier_str_mv ALMEIDA FILHO, Luiz C. P. et al. First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin-trypsin inhibitor purified from Lonchocarpus sericeus seeds. Pest Manag Sci, [s. l.], v. 74, n. 6, p. 1362-1373, 2018.
url http://www.repositorio.ufc.br/handle/riufc/62916
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Pest Manag Sci
publisher.none.fl_str_mv Pest Manag Sci
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Federal do Ceará (UFC)
instname:Universidade Federal do Ceará (UFC)
instacron:UFC
instname_str Universidade Federal do Ceará (UFC)
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institution UFC
reponame_str Repositório Institucional da Universidade Federal do Ceará (UFC)
collection Repositório Institucional da Universidade Federal do Ceará (UFC)
repository.name.fl_str_mv Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)
repository.mail.fl_str_mv bu@ufc.br || repositorio@ufc.br
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