BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)

Detalhes bibliográficos
Autor(a) principal: Teixeira, Denise Gonçalves
Data de Publicação: 2016
Outros Autores: Borges, Lígia Miranda Ferreira, Mastrângelo, Thiago de Araújo, Monteiro, Valdirene Neves
Tipo de documento: Artigo
Idioma: por
Título da fonte: Ciência animal brasileira (Online)
Texto Completo: https://revistas.ufg.br/vet/article/view/37176
Resumo: The species Cochliomyia hominivorax, also known as screwworm fly, is an obligate parasite of warm- blooded animals and its geographic range extends thoughout South America, except Chile. This fly causes significant economic losses and has great importance in Brazil. Few studies have focused on the excretion and secretion products of this species, and this research aimed to study the enzymes present in the secretion and excretion (E/S) products of the three larval instars of C. hominivorax. The E/S profile of proteins was obtained by polyacrylamide gel electrophoresis and proteolytic activity was analyzed using gelatin, azocasein and Na-benzoyl-arginine-nitroanilide as substrates.  In E/S products of the three instars, proteins were detected with an apparent molecular weight ranging between 116 and 20 kDa. In the azocasein assay, at different pH ranges, the major proteolytic activity occurred at pH 7.5 for all larval instars. Assays were performed using the same substrates   in which the samples were treated with the inhibitors Benzamidine, Pepstatin A, 4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride (AEBSF), N-?-tosyl-L-lysine chloromethyl ketone (TLCK), N-?- tosyl-L-phenylalanine chloromethyl ketone (TPCK), Ethylenediamine tetraacetic acid (EDTA), and Leupeptin-trans-Epoxysuccinyl-leucylamido(4-guanidino) butane (E-64). Proteinases present in the E/S product of first larvae instar are mostly serine trypsin and chymotrypsin proteases, whereas for second and third instars serine proteases and aspartyl proteases were predominantly observed. Biochemical characterization of E/S products of all larval stages of C. hominivorax helps to improve the understanding of the physiology and the interaction of this parasite with host tissues.Keywords: Enzyme; fly; myiasis; parasites.
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spelling BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)CARACTERIZAÇÃO BIOQUÍMICA DO PRODUTO DE EXCREÇÃO/ SECREÇÃO DE LARVAS DE Cochliomyia hominivorax (DIPTERA: CALLIPHORIDAE)ParasithologySanidade AnimalThe species Cochliomyia hominivorax, also known as screwworm fly, is an obligate parasite of warm- blooded animals and its geographic range extends thoughout South America, except Chile. This fly causes significant economic losses and has great importance in Brazil. Few studies have focused on the excretion and secretion products of this species, and this research aimed to study the enzymes present in the secretion and excretion (E/S) products of the three larval instars of C. hominivorax. The E/S profile of proteins was obtained by polyacrylamide gel electrophoresis and proteolytic activity was analyzed using gelatin, azocasein and Na-benzoyl-arginine-nitroanilide as substrates.  In E/S products of the three instars, proteins were detected with an apparent molecular weight ranging between 116 and 20 kDa. In the azocasein assay, at different pH ranges, the major proteolytic activity occurred at pH 7.5 for all larval instars. Assays were performed using the same substrates   in which the samples were treated with the inhibitors Benzamidine, Pepstatin A, 4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride (AEBSF), N-?-tosyl-L-lysine chloromethyl ketone (TLCK), N-?- tosyl-L-phenylalanine chloromethyl ketone (TPCK), Ethylenediamine tetraacetic acid (EDTA), and Leupeptin-trans-Epoxysuccinyl-leucylamido(4-guanidino) butane (E-64). Proteinases present in the E/S product of first larvae instar are mostly serine trypsin and chymotrypsin proteases, whereas for second and third instars serine proteases and aspartyl proteases were predominantly observed. Biochemical characterization of E/S products of all larval stages of C. hominivorax helps to improve the understanding of the physiology and the interaction of this parasite with host tissues.Keywords: Enzyme; fly; myiasis; parasites.A espécie Cochliomyia hominivorax, conhecida popularmente como mosca da bicheira, é um parasita obrigatório de animais de sangue quente e sua distribuição geográfica estende-se por toda a América do Sul, excetuando-se o Chile. O parasitismo por esta mosca provoca perdas econômicas significativas e tem grande importância no Brasil. São poucos os estudos com foco nos produtos de excreção e secreção desta espécie e este trabalho teve como objetivo estudar as enzimas presentes  no produto de secreção e excreção (E/S) dos três estádios larvais de C. hominivorax. O perfil de proteínas foi obtido por eletroforese em gel de poliacrilamida e a atividade proteolítica foi analisada utilizando-se gelatina, azocaseína e Na-benzoil-arginina-nitroanilida (BAPNA) como substrato. Nos produtos de E/S dos três estádios, as proteínas foram detectadas com um peso molecular aparente que variou entre 116 e 20 kDa. No ensaio de azocaseína, em diferentes faixas de pH, a maior atividade proteolítica ocorreu em pH 7,5 para todos os estádios larvais. Os ensaios foram realizados usando- se estes mesmos substratos e as amostras foram tratadas com os inibidores Benzamidina, Pepstatin A, 4-(2-aminoetil)benzenosulfonil fluoreto hidrocloreto (AEBSF), N-?-tosil-L-lisina clorometil cetona (TLCK), N-?-tosil-L-fenilalanina clorometil cetona (TPCK), Ácido etilenodiamino tetra acético (EDTA), Leupeptina e Trans-epoxysuccinyl L-leucylamido-4-guanidino butano (E-64). As proteinases presentes nos produtos E/S de L1 são em sua maioria serina proteases do tipo tripsina e quimotripsina, enquanto que para os produtos E/S de L2 e L3 foi evidenciada a presença de serina proteases e aspartil proteases.Palavras-chave: enzima; miíase; mosca; parasitas.Universidade Federal de Goiás2016-10-28info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionResearchAvaliado por paresPesquisa Científicaapplication/pdftext/htmlhttps://revistas.ufg.br/vet/article/view/3717610.1590/cab17437176Brazilian Animal Science/ Ciência Animal Brasileira; Vol. 17 No. 4 (2016); 581-592Ciência Animal Brasileira / Brazilian Animal Science; v. 17 n. 4 (2016); 581-5921809-68911518-2797reponame:Ciência animal brasileira (Online)instname:Universidade Federal de Goiás (UFG)instacron:UFGporhttps://revistas.ufg.br/vet/article/view/37176/21919https://revistas.ufg.br/vet/article/view/37176/21920Teixeira, Denise GonçalvesBorges, Lígia Miranda FerreiraMastrângelo, Thiago de AraújoMonteiro, Valdirene Nevesinfo:eu-repo/semantics/openAccess2016-11-03T19:53:25Zoai:ojs.revistas.ufg.br:article/37176Revistahttps://revistas.ufg.br/vetPUBhttps://revistas.ufg.br/vet/oai||revistacab@gmail.com1809-68911518-2797opendoar:2024-05-21T19:56:11.156874Ciência animal brasileira (Online) - Universidade Federal de Goiás (UFG)true
dc.title.none.fl_str_mv BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
CARACTERIZAÇÃO BIOQUÍMICA DO PRODUTO DE EXCREÇÃO/ SECREÇÃO DE LARVAS DE Cochliomyia hominivorax (DIPTERA: CALLIPHORIDAE)
title BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
spellingShingle BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
Teixeira, Denise Gonçalves
Parasithology
Sanidade Animal
title_short BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
title_full BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
title_fullStr BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
title_full_unstemmed BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
title_sort BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
author Teixeira, Denise Gonçalves
author_facet Teixeira, Denise Gonçalves
Borges, Lígia Miranda Ferreira
Mastrângelo, Thiago de Araújo
Monteiro, Valdirene Neves
author_role author
author2 Borges, Lígia Miranda Ferreira
Mastrângelo, Thiago de Araújo
Monteiro, Valdirene Neves
author2_role author
author
author
dc.contributor.author.fl_str_mv Teixeira, Denise Gonçalves
Borges, Lígia Miranda Ferreira
Mastrângelo, Thiago de Araújo
Monteiro, Valdirene Neves
dc.subject.por.fl_str_mv Parasithology
Sanidade Animal
topic Parasithology
Sanidade Animal
description The species Cochliomyia hominivorax, also known as screwworm fly, is an obligate parasite of warm- blooded animals and its geographic range extends thoughout South America, except Chile. This fly causes significant economic losses and has great importance in Brazil. Few studies have focused on the excretion and secretion products of this species, and this research aimed to study the enzymes present in the secretion and excretion (E/S) products of the three larval instars of C. hominivorax. The E/S profile of proteins was obtained by polyacrylamide gel electrophoresis and proteolytic activity was analyzed using gelatin, azocasein and Na-benzoyl-arginine-nitroanilide as substrates.  In E/S products of the three instars, proteins were detected with an apparent molecular weight ranging between 116 and 20 kDa. In the azocasein assay, at different pH ranges, the major proteolytic activity occurred at pH 7.5 for all larval instars. Assays were performed using the same substrates   in which the samples were treated with the inhibitors Benzamidine, Pepstatin A, 4-(2-Aminoethyl) benzenesulfonyl fluoride hydrochloride (AEBSF), N-?-tosyl-L-lysine chloromethyl ketone (TLCK), N-?- tosyl-L-phenylalanine chloromethyl ketone (TPCK), Ethylenediamine tetraacetic acid (EDTA), and Leupeptin-trans-Epoxysuccinyl-leucylamido(4-guanidino) butane (E-64). Proteinases present in the E/S product of first larvae instar are mostly serine trypsin and chymotrypsin proteases, whereas for second and third instars serine proteases and aspartyl proteases were predominantly observed. Biochemical characterization of E/S products of all larval stages of C. hominivorax helps to improve the understanding of the physiology and the interaction of this parasite with host tissues.Keywords: Enzyme; fly; myiasis; parasites.
publishDate 2016
dc.date.none.fl_str_mv 2016-10-28
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Research
Avaliado por pares
Pesquisa Científica
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://revistas.ufg.br/vet/article/view/37176
10.1590/cab17437176
url https://revistas.ufg.br/vet/article/view/37176
identifier_str_mv 10.1590/cab17437176
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv https://revistas.ufg.br/vet/article/view/37176/21919
https://revistas.ufg.br/vet/article/view/37176/21920
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
text/html
dc.publisher.none.fl_str_mv Universidade Federal de Goiás
publisher.none.fl_str_mv Universidade Federal de Goiás
dc.source.none.fl_str_mv Brazilian Animal Science/ Ciência Animal Brasileira; Vol. 17 No. 4 (2016); 581-592
Ciência Animal Brasileira / Brazilian Animal Science; v. 17 n. 4 (2016); 581-592
1809-6891
1518-2797
reponame:Ciência animal brasileira (Online)
instname:Universidade Federal de Goiás (UFG)
instacron:UFG
instname_str Universidade Federal de Goiás (UFG)
instacron_str UFG
institution UFG
reponame_str Ciência animal brasileira (Online)
collection Ciência animal brasileira (Online)
repository.name.fl_str_mv Ciência animal brasileira (Online) - Universidade Federal de Goiás (UFG)
repository.mail.fl_str_mv ||revistacab@gmail.com
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