Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Repositório Institucional da UFG |
Texto Completo: | http://repositorio.bc.ufg.br/tede/handle/tede/7714 |
Resumo: | Paracoccidioides spp. are thermodymorphic fungi that when inhaled by humans, these conidia find a favorable environment, changing to the yeast phase and becoming pathogenic causing paracoccidioidomycosis (PCM), one of the most prevalent systemic mycoses in Brazil. Some antifungals are used in the treatment of PCM. Treatment depends on the patient's progression and tolerability of each drug, but their treatment may be for long periods and cause various side effects in the patient. The chiquimate pathway is coordinated by 7 enzymes that perform consecutive steps to convert erythrose-4-phosphate and phosphoenol pyruvate (PEP) into chorismate. In microorganisms, this pathway is involved in the production of the amino acids phenylalanine, tyrosine and tryptophan; These amino acids are essential to the maintenance of these organisms. In this work, pGEX4T3 vector cloning and heterologous expression of Pb18 EPSP synthase belonging to the chiquimate pathway were performed. This protein was expressed in E. coli (DE3) strain and purified. Antibodies were produced for expression analysis of the protein in Western blot. The modeling of EPSP synthase was performed aiming to identify the amino acids involved in the active site. The pull down-GST assay with soluble Pb18 proteins allowed the identification of 40 proteins that interact with EPSP synthase. These proteins belong to different functional categories, which are involved with the availability of phosphoenol pyruvate, the substrate necessary for the functioning of the chiquimate pathway. |
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Pereira, Maristelahttp://lattes.cnpq.br/1345781867765758Pereira, MaristelaLacerda, Elisângela de Paula SilveiraNeves, Bruno Juniorhttp://lattes.cnpq.br/1779239304574744Costa, Wanderson Lucas da2017-09-15T13:46:23Z2017-08-07COSTA, W. L. Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis. 2017. 85 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017.http://repositorio.bc.ufg.br/tede/handle/tede/7714ark:/38995/001300000ds7gParacoccidioides spp. are thermodymorphic fungi that when inhaled by humans, these conidia find a favorable environment, changing to the yeast phase and becoming pathogenic causing paracoccidioidomycosis (PCM), one of the most prevalent systemic mycoses in Brazil. Some antifungals are used in the treatment of PCM. Treatment depends on the patient's progression and tolerability of each drug, but their treatment may be for long periods and cause various side effects in the patient. The chiquimate pathway is coordinated by 7 enzymes that perform consecutive steps to convert erythrose-4-phosphate and phosphoenol pyruvate (PEP) into chorismate. In microorganisms, this pathway is involved in the production of the amino acids phenylalanine, tyrosine and tryptophan; These amino acids are essential to the maintenance of these organisms. In this work, pGEX4T3 vector cloning and heterologous expression of Pb18 EPSP synthase belonging to the chiquimate pathway were performed. This protein was expressed in E. coli (DE3) strain and purified. Antibodies were produced for expression analysis of the protein in Western blot. The modeling of EPSP synthase was performed aiming to identify the amino acids involved in the active site. The pull down-GST assay with soluble Pb18 proteins allowed the identification of 40 proteins that interact with EPSP synthase. These proteins belong to different functional categories, which are involved with the availability of phosphoenol pyruvate, the substrate necessary for the functioning of the chiquimate pathway.Paracoccidioides spp. são fungos termodimórficos que ao serem inalados pelo ser humano, esses conídios encontram um ambiente propício, mudando para a fase de levedura e tornando-se patogênico causando a paracoccidioidomicose (PCM), umas das micoses sistêmicas de maior prevalência no Brasil. Alguns antifúngicos são empregados no tratamento da PCM. O tratamento depende do avanço da doença e da capacidade de tolerância do paciente a cada medicamento, mas o seu tratamento pode ser por longos períodos e causando diversos efeitos colaterais no paciente. A via do chiquimato é coordenada pela ação de 7 enzimas que realizam passos consecutivos para transformar a eritrose-4-fosfato e fosfoenol piruvato (PEP) em corismato. Em micro-organismos, esta via está envolvida com a produção dos aminoácidos fenilalanina, tirosina e triptofano; estes aminoácidos são essenciais à manutenção desses organismos. Neste trabalho foi realizado a clonagem em vetor pGEX4T3 e expressão heteróloga da EPSP–sintase de Pb18 pertencente à via do chiquimato. Essa proteína foi expressa em linhagem E. coli (DE3) e purificada. Os anticorpos foram produzidos para análise da expressão da proteína em Western blot. A modelagem da EPSP-sintase foi realizada visando identificar os aminoácidos envolvidos no sítio ativo. O ensaio de pull down-GST com proteínas solúveis de Pb18 possibilitou a identificação de 40 proteínas que interagem com EPSP-sintase. Essas proteínas pertencem a diferentes categorias funcionais, as quais estão envolvidas com a disponibilidade de fosfoenol piruvato, substrato necessário para o funcionamento da via do chiquimato.Submitted by Cássia Santos (cassia.bcufg@gmail.com) on 2017-09-01T13:05:01Z No. of bitstreams: 2 Dissertação - Wanderson Lucas da Costa - 2017.pdf: 3043089 bytes, checksum: 32c1b9c81dae778ab37d939fdba41eb5 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Approved for entry into archive by Luciana Ferreira (lucgeral@gmail.com) on 2017-09-15T13:46:23Z (GMT) No. of bitstreams: 2 Dissertação - Wanderson Lucas da Costa - 2017.pdf: 3043089 bytes, checksum: 32c1b9c81dae778ab37d939fdba41eb5 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Made available in DSpace on 2017-09-15T13:46:23Z (GMT). No. of bitstreams: 2 Dissertação - Wanderson Lucas da Costa - 2017.pdf: 3043089 bytes, checksum: 32c1b9c81dae778ab37d939fdba41eb5 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5) Previous issue date: 2017-08-07Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfporUniversidade Federal de GoiásPrograma de Pós-graduação em Genética e Biologia MolecularUFGBrasilInstituto de Ciências Biológicas - ICB (RG)http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessExpressão heterólogaEPSP-sintaseModelagemParacoccidioides brasiliensisPull down-GSTVia do chiquimatoHeterologus expressionEPSP-synthaseModelingParacoccidioides brasiliensisPull down-GSTShikimate pathwayGENETICA::GENETICA MOLECULAR E DE MICROORGANISMOSClonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensisCloning and heterologous expression, modeling and intermolecular interactions of enolpiruvilchiquimato 3-phosphate synthase from Paracoccidioides brasiliensisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis7015780075895009588600600600600-3872772117827373404-7683082515614575372075167498588264571reponame:Repositório Institucional da UFGinstname:Universidade Federal de Goiás (UFG)instacron:UFGCC-LICENSElicense_urllicense_urltext/plain; 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dc.title.eng.fl_str_mv |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
dc.title.alternative.eng.fl_str_mv |
Cloning and heterologous expression, modeling and intermolecular interactions of enolpiruvilchiquimato 3-phosphate synthase from Paracoccidioides brasiliensis |
title |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
spellingShingle |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis Costa, Wanderson Lucas da Expressão heteróloga EPSP-sintase Modelagem Paracoccidioides brasiliensis Pull down-GST Via do chiquimato Heterologus expression EPSP-synthase Modeling Paracoccidioides brasiliensis Pull down-GST Shikimate pathway GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
title_short |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
title_full |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
title_fullStr |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
title_full_unstemmed |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
title_sort |
Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis |
author |
Costa, Wanderson Lucas da |
author_facet |
Costa, Wanderson Lucas da |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Pereira, Maristela |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/1345781867765758 |
dc.contributor.referee1.fl_str_mv |
Pereira, Maristela |
dc.contributor.referee2.fl_str_mv |
Lacerda, Elisângela de Paula Silveira |
dc.contributor.referee3.fl_str_mv |
Neves, Bruno Junior |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/1779239304574744 |
dc.contributor.author.fl_str_mv |
Costa, Wanderson Lucas da |
contributor_str_mv |
Pereira, Maristela Pereira, Maristela Lacerda, Elisângela de Paula Silveira Neves, Bruno Junior |
dc.subject.por.fl_str_mv |
Expressão heteróloga EPSP-sintase Modelagem Paracoccidioides brasiliensis Pull down-GST Via do chiquimato |
topic |
Expressão heteróloga EPSP-sintase Modelagem Paracoccidioides brasiliensis Pull down-GST Via do chiquimato Heterologus expression EPSP-synthase Modeling Paracoccidioides brasiliensis Pull down-GST Shikimate pathway GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
dc.subject.eng.fl_str_mv |
Heterologus expression EPSP-synthase Modeling Paracoccidioides brasiliensis Pull down-GST Shikimate pathway |
dc.subject.cnpq.fl_str_mv |
GENETICA::GENETICA MOLECULAR E DE MICROORGANISMOS |
description |
Paracoccidioides spp. are thermodymorphic fungi that when inhaled by humans, these conidia find a favorable environment, changing to the yeast phase and becoming pathogenic causing paracoccidioidomycosis (PCM), one of the most prevalent systemic mycoses in Brazil. Some antifungals are used in the treatment of PCM. Treatment depends on the patient's progression and tolerability of each drug, but their treatment may be for long periods and cause various side effects in the patient. The chiquimate pathway is coordinated by 7 enzymes that perform consecutive steps to convert erythrose-4-phosphate and phosphoenol pyruvate (PEP) into chorismate. In microorganisms, this pathway is involved in the production of the amino acids phenylalanine, tyrosine and tryptophan; These amino acids are essential to the maintenance of these organisms. In this work, pGEX4T3 vector cloning and heterologous expression of Pb18 EPSP synthase belonging to the chiquimate pathway were performed. This protein was expressed in E. coli (DE3) strain and purified. Antibodies were produced for expression analysis of the protein in Western blot. The modeling of EPSP synthase was performed aiming to identify the amino acids involved in the active site. The pull down-GST assay with soluble Pb18 proteins allowed the identification of 40 proteins that interact with EPSP synthase. These proteins belong to different functional categories, which are involved with the availability of phosphoenol pyruvate, the substrate necessary for the functioning of the chiquimate pathway. |
publishDate |
2017 |
dc.date.accessioned.fl_str_mv |
2017-09-15T13:46:23Z |
dc.date.issued.fl_str_mv |
2017-08-07 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
COSTA, W. L. Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis. 2017. 85 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017. |
dc.identifier.uri.fl_str_mv |
http://repositorio.bc.ufg.br/tede/handle/tede/7714 |
dc.identifier.dark.fl_str_mv |
ark:/38995/001300000ds7g |
identifier_str_mv |
COSTA, W. L. Clonagem e expressão heteróloga, modelagem e interações intermoleculares da enolpiruvilchiquimato 3-fosfato sintase de Paracoccidioides brasiliensis. 2017. 85 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2017. ark:/38995/001300000ds7g |
url |
http://repositorio.bc.ufg.br/tede/handle/tede/7714 |
dc.language.iso.fl_str_mv |
por |
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por |
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7015780075895009588 |
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600 600 600 600 |
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-3872772117827373404 |
dc.relation.cnpq.fl_str_mv |
-768308251561457537 |
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2075167498588264571 |
dc.rights.driver.fl_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-nd/4.0/ |
eu_rights_str_mv |
openAccess |
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application/pdf |
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Universidade Federal de Goiás |
dc.publisher.program.fl_str_mv |
Programa de Pós-graduação em Genética e Biologia Molecular |
dc.publisher.initials.fl_str_mv |
UFG |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
Instituto de Ciências Biológicas - ICB (RG) |
publisher.none.fl_str_mv |
Universidade Federal de Goiás |
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