Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Tipo de documento: | Dissertação |
Idioma: | por |
Título da fonte: | Repositório Institucional da UFG |
Texto Completo: | http://repositorio.bc.ufg.br/tede/handle/tede/9281 |
Resumo: | The genus Paracoccidioides comprises thermodymorphic ascomycete’s fungi, causative agents of Paracoccidioidomycosis (PCM). PCM is an endemic granulomatous systemic mycosis in Latin America. The pathogen ability to interact and adhere to host surface structures is critical to the colonization, invasion, growth, and hematogenous spread of the fungus to tissues. Fungi use a variety of surface molecules to bind to the components of the host's extracellular matrix and defense cells, such as macrophages, so they can survive in these environments. A total of 94 cell wall proteins of Paracoccidioides spp. interacting with macrophages were identified through mass spectrometry studies. In this sense it becomes important the production of those possible adhesins via heterologous expression and localization of these proteins, aiming to perform adhesion studies. Therefore, HSP30 and peroxisomal catalase proteins of Paracoccidioides brasiliensis were expressed in a bacterial heterologous system, Escherichia coli. Open reading frames (ORFs) of the genes encoding HSP30 and peroxisomal catalase were cloned into pGEX-4T3 expression vector and the respective clones were used in the transformation of E. coli pLySs cells. The recombinant proteins were used in the production of polyclonal antibodies in mice. Anti-HSP30 and anti-CatP polyclonal antibodies were used in immunofluorescence assays, to obtain confirmation of the cellular location of HSP30 and CatP proteins. The obtained data allowed the localization of those proteins in the cell wall of the fungi cells, corroborating with the proteomic analyzes. The aim of this work is to perform additional macrophage interaction experiments to evaluate the potential of both proteins as adhesins. |
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Soares, Célia Maria de Almeidahttp://lattes.cnpq.br/8539946335852637Tomazett, Mariana Vieirahttp://lattes.cnpq.br/1754626527596461Dias, Fátima RibeiroPaccez, Juliano DomiraciSoares, Célia Maria de Almeidahttp://lattes.cnpq.br/7938638213946544Pereira, Christie Ataides2019-02-11T10:24:46Z2018-03-09PEREIRA, C. A. Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos. 2018. 67 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2018.http://repositorio.bc.ufg.br/tede/handle/tede/9281The genus Paracoccidioides comprises thermodymorphic ascomycete’s fungi, causative agents of Paracoccidioidomycosis (PCM). PCM is an endemic granulomatous systemic mycosis in Latin America. The pathogen ability to interact and adhere to host surface structures is critical to the colonization, invasion, growth, and hematogenous spread of the fungus to tissues. Fungi use a variety of surface molecules to bind to the components of the host's extracellular matrix and defense cells, such as macrophages, so they can survive in these environments. A total of 94 cell wall proteins of Paracoccidioides spp. interacting with macrophages were identified through mass spectrometry studies. In this sense it becomes important the production of those possible adhesins via heterologous expression and localization of these proteins, aiming to perform adhesion studies. Therefore, HSP30 and peroxisomal catalase proteins of Paracoccidioides brasiliensis were expressed in a bacterial heterologous system, Escherichia coli. Open reading frames (ORFs) of the genes encoding HSP30 and peroxisomal catalase were cloned into pGEX-4T3 expression vector and the respective clones were used in the transformation of E. coli pLySs cells. The recombinant proteins were used in the production of polyclonal antibodies in mice. Anti-HSP30 and anti-CatP polyclonal antibodies were used in immunofluorescence assays, to obtain confirmation of the cellular location of HSP30 and CatP proteins. The obtained data allowed the localization of those proteins in the cell wall of the fungi cells, corroborating with the proteomic analyzes. The aim of this work is to perform additional macrophage interaction experiments to evaluate the potential of both proteins as adhesins.O gênero Paracoccidioides compreende fungos ascomicetos termodimórficos, que causam a doença Paracoccidioidomicose (PCM). A PCM é uma micose sistêmica granulomatosa e endêmica na América Latina. A capacidade do patógeno de interagir e aderir à matriz extracelular do hospedeiro é fundamental para a colonização, invasão, crescimento e disseminação hematogênica do fungo para tecidos. Os fungos utilizam uma variedade de moléculas de superfície para se aderirem à componentes da matriz extracelular do hospedeiro e células de defesa, como macrófagos, podendo assim sobreviver nesses ambientes. Foi identificado por meio de estudos de espectrometria de massa, um total de 94 proteínas da parede celular de Paracoccidioides spp. interagindo com macrófagos. Nesse sentido torna-se importante a produção dessas possíveis adesinas via expressão heteróloga e localização dessas proteínas, visando estudos posteriores de adesão. Neste estudo, foram expressas as proteínas HSP30 e catalase peroxissomal de Paracoccidioides brasiliensis em sistema heterólogo bacteriano, Escherichia coli. Os quadros abertos de leitura (ORFs) dos genes codificadores de HSP30 e catalase peroxissomal foram clonados em vetor de expressão pGEX-4T3 e os respectivos clones foram utilizados na transformação de células de E. coli pLySs. As proteínas recombinantes resultantes foram utilizadas na produção de anticorpos policlonais,em camundongos. Os anticorpos policlonais anti-HSP30 e anti-CatP foram utilizados em ensaios de imunofluorescência para confirmação da localização celular das proteínas HSP30 e CatP. Com os resultados pode-se observar que as proteínas estão localizadas na parede celular do fungo corroborando assim com os dados de análises proteômicas previamente publicados. A perspectiva deste trabalho é realizar experimentos adicionais de interação com macrófagos para avaliar o potencial de ambas as proteínas como adesinas.Submitted by Luciana Ferreira (lucgeral@gmail.com) on 2019-02-11T10:19:53Z No. of bitstreams: 2 Dissertação - Christie Ataides Pereira - 2018.pdf: 2029195 bytes, checksum: b9fbd3f81e3957f4e060b51e3f5c3392 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Approved for entry into archive by Luciana Ferreira (lucgeral@gmail.com) on 2019-02-11T10:24:46Z (GMT) No. of bitstreams: 2 Dissertação - Christie Ataides Pereira - 2018.pdf: 2029195 bytes, checksum: b9fbd3f81e3957f4e060b51e3f5c3392 (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Made available in DSpace on 2019-02-11T10:24:46Z (GMT). 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dc.title.eng.fl_str_mv |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
dc.title.alternative.eng.fl_str_mv |
Heterologous expression and immunolocalization of HSP30 and peroxisomal catalase proteins in the wall of Paracoccidioides spp. interacting with macrophages |
title |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
spellingShingle |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos Pereira, Christie Ataides Adesinas Catalase peroxissomal Paracoccidioides HSP30 Adhesins HSP30 Peroxisomal catalase Paracoccidioides BIOQUIMICA::BIOLOGIA MOLECULAR |
title_short |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
title_full |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
title_fullStr |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
title_full_unstemmed |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
title_sort |
Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos |
author |
Pereira, Christie Ataides |
author_facet |
Pereira, Christie Ataides |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
Soares, Célia Maria de Almeida |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/8539946335852637 |
dc.contributor.advisor-co1.fl_str_mv |
Tomazett, Mariana Vieira |
dc.contributor.advisor-co1Lattes.fl_str_mv |
http://lattes.cnpq.br/1754626527596461 |
dc.contributor.referee1.fl_str_mv |
Dias, Fátima Ribeiro |
dc.contributor.referee2.fl_str_mv |
Paccez, Juliano Domiraci |
dc.contributor.referee3.fl_str_mv |
Soares, Célia Maria de Almeida |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/7938638213946544 |
dc.contributor.author.fl_str_mv |
Pereira, Christie Ataides |
contributor_str_mv |
Soares, Célia Maria de Almeida Tomazett, Mariana Vieira Dias, Fátima Ribeiro Paccez, Juliano Domiraci Soares, Célia Maria de Almeida |
dc.subject.por.fl_str_mv |
Adesinas Catalase peroxissomal Paracoccidioides HSP30 |
topic |
Adesinas Catalase peroxissomal Paracoccidioides HSP30 Adhesins HSP30 Peroxisomal catalase Paracoccidioides BIOQUIMICA::BIOLOGIA MOLECULAR |
dc.subject.eng.fl_str_mv |
Adhesins HSP30 Peroxisomal catalase Paracoccidioides |
dc.subject.cnpq.fl_str_mv |
BIOQUIMICA::BIOLOGIA MOLECULAR |
description |
The genus Paracoccidioides comprises thermodymorphic ascomycete’s fungi, causative agents of Paracoccidioidomycosis (PCM). PCM is an endemic granulomatous systemic mycosis in Latin America. The pathogen ability to interact and adhere to host surface structures is critical to the colonization, invasion, growth, and hematogenous spread of the fungus to tissues. Fungi use a variety of surface molecules to bind to the components of the host's extracellular matrix and defense cells, such as macrophages, so they can survive in these environments. A total of 94 cell wall proteins of Paracoccidioides spp. interacting with macrophages were identified through mass spectrometry studies. In this sense it becomes important the production of those possible adhesins via heterologous expression and localization of these proteins, aiming to perform adhesion studies. Therefore, HSP30 and peroxisomal catalase proteins of Paracoccidioides brasiliensis were expressed in a bacterial heterologous system, Escherichia coli. Open reading frames (ORFs) of the genes encoding HSP30 and peroxisomal catalase were cloned into pGEX-4T3 expression vector and the respective clones were used in the transformation of E. coli pLySs cells. The recombinant proteins were used in the production of polyclonal antibodies in mice. Anti-HSP30 and anti-CatP polyclonal antibodies were used in immunofluorescence assays, to obtain confirmation of the cellular location of HSP30 and CatP proteins. The obtained data allowed the localization of those proteins in the cell wall of the fungi cells, corroborating with the proteomic analyzes. The aim of this work is to perform additional macrophage interaction experiments to evaluate the potential of both proteins as adhesins. |
publishDate |
2018 |
dc.date.issued.fl_str_mv |
2018-03-09 |
dc.date.accessioned.fl_str_mv |
2019-02-11T10:24:46Z |
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 |
PEREIRA, C. A. Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos. 2018. 67 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2018. |
dc.identifier.uri.fl_str_mv |
http://repositorio.bc.ufg.br/tede/handle/tede/9281 |
identifier_str_mv |
PEREIRA, C. A. Expressão heterológa e imunolocalização das proteínas HSP30 e catalase peroxissomal identificadas na parede de Paracoccidioides spp. interagindo com macrófagos. 2018. 67 f. Dissertação (Mestrado em Genética e Biologia Molecular) - Universidade Federal de Goiás, Goiânia, 2018. |
url |
http://repositorio.bc.ufg.br/tede/handle/tede/9281 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.program.fl_str_mv |
-3983316729959641468 |
dc.relation.confidence.fl_str_mv |
600 600 600 600 |
dc.relation.department.fl_str_mv |
-3872772117827373404 |
dc.relation.cnpq.fl_str_mv |
3962143990328052072 |
dc.relation.sponsorship.fl_str_mv |
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 |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Federal de Goiás |
dc.publisher.program.fl_str_mv |
Programa de Pós-graduação em Genética e Biologia Molecular (ICB) |
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 |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UFG instname:Universidade Federal de Goiás (UFG) instacron:UFG |
instname_str |
Universidade Federal de Goiás (UFG) |
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UFG |
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UFG |
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Repositório Institucional da UFG |
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Repositório Institucional da UFG |
bitstream.url.fl_str_mv |
http://repositorio.bc.ufg.br/tede/bitstreams/f30ffdac-77cd-42b6-97ff-2a5aa2560682/download http://repositorio.bc.ufg.br/tede/bitstreams/09456bfc-7f43-45d1-a57c-6b717d99e7bf/download http://repositorio.bc.ufg.br/tede/bitstreams/f6a854a5-6424-4396-991b-a47c9b4f463d/download http://repositorio.bc.ufg.br/tede/bitstreams/cd1e09ef-b2ce-42eb-9223-70fd655f5fc7/download http://repositorio.bc.ufg.br/tede/bitstreams/f633ad4c-79d3-43aa-9a22-63dcdc5d988b/download http://repositorio.bc.ufg.br/tede/bitstreams/a89a8fe9-debd-4161-9d69-e23798fc276d/download http://repositorio.bc.ufg.br/tede/bitstreams/c20f230a-e589-4739-a897-137b5dcd89cd/download |
bitstream.checksum.fl_str_mv |
bd3efa91386c1718a7f26a329fdcb468 4afdbb8c545fd630ea7db775da747b2f d41d8cd98f00b204e9800998ecf8427e d41d8cd98f00b204e9800998ecf8427e b9fbd3f81e3957f4e060b51e3f5c3392 38037648937cccba57adacea722a7190 ee47fa484a6173215ed3ec43eb175aa4 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 MD5 MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UFG - Universidade Federal de Goiás (UFG) |
repository.mail.fl_str_mv |
tasesdissertacoes.bc@ufg.br |
_version_ |
1798044361123954688 |