BIOCHEMISTRY CHARACTERIZATION OF EXCRETION / SECRETION PRODUCT OF Cochliomyia hominivorax LARVAE (DIPTERA : CALLIPHORIDAE)
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , |
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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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 |
_version_ |
1799874788850663424 |