Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides

Detalhes bibliográficos
Autor(a) principal: Chaves, Edilânia Gomes Araújo
Data de Publicação: 2013
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Repositório Institucional da UFG
Texto Completo: http://repositorio.bc.ufg.br/tede/handle/tede/6856
Resumo: Paracoccicoidioides is the etiological agent of paracoccidioidomycosis (PCM), a disease considered one of the main causes of mortality among systemic mycoses in Brazil. The success in establishing of the infection is related with the ability of fungus to adhere and degrade components of the extracellular matrix (ECM). Human plasminogen (hPlg) is a protein of blood plasma of the host that presents fibrinolytic activity when activated into plasmin. Many pathogens are able to subvert the plasminogen/plasmin system using linker molecules and promote the degradation of tissue barriers. In this work, we identified through Far Western and proteomic analysis, a total of 15 proteins secreted of Paracoccidioides that are plasminogen binding proteins. Those proteins are probable targets of the interaction of the fungus with the host and could contribute to the invasiveness of the fungus. The fructose 1,6-biphosphate aldolase was described in other organisms such as plasminogen binder and presentes participation in the adherence of Paracoccidioides to host cells. This protein selected for validation tests and their presence was observed on the surface and secretory vesicles of the fungus. FBA confirm the ability to convert plasminogen to plasmin in the presence of tissue plasminogen activator (tPA) and this interaction promoted the degradation of fibrin. In infection assays, the addition of antibodies blocking the FBA binding site reduced the interaction of the fungus with macrophages and the interaction of FBA with Plg increased the rate of cell invasion. These data suggest that the FBA can contribute to adhesion, invasion and spread process of the fungus.
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spelling Soares, Célia Maria de Almeidahttp://lattes.cnpq.br/8539946335852637Bailão, Alexandre MeloAmaral, André Corrêahttp://lattes.cnpq.br/1438544283655466Chaves, Edilânia Gomes Araújo2017-02-17T16:53:18Z2013-03-20CHAVES, E. G. A. Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides. 2013. 59 f. Dissertação (mestrado em Medicina Tropical e Saúde Pública) - Universidade Federal de Goiás, Goiânia, 2013.http://repositorio.bc.ufg.br/tede/handle/tede/6856Paracoccicoidioides is the etiological agent of paracoccidioidomycosis (PCM), a disease considered one of the main causes of mortality among systemic mycoses in Brazil. The success in establishing of the infection is related with the ability of fungus to adhere and degrade components of the extracellular matrix (ECM). Human plasminogen (hPlg) is a protein of blood plasma of the host that presents fibrinolytic activity when activated into plasmin. Many pathogens are able to subvert the plasminogen/plasmin system using linker molecules and promote the degradation of tissue barriers. In this work, we identified through Far Western and proteomic analysis, a total of 15 proteins secreted of Paracoccidioides that are plasminogen binding proteins. Those proteins are probable targets of the interaction of the fungus with the host and could contribute to the invasiveness of the fungus. The fructose 1,6-biphosphate aldolase was described in other organisms such as plasminogen binder and presentes participation in the adherence of Paracoccidioides to host cells. This protein selected for validation tests and their presence was observed on the surface and secretory vesicles of the fungus. FBA confirm the ability to convert plasminogen to plasmin in the presence of tissue plasminogen activator (tPA) and this interaction promoted the degradation of fibrin. In infection assays, the addition of antibodies blocking the FBA binding site reduced the interaction of the fungus with macrophages and the interaction of FBA with Plg increased the rate of cell invasion. These data suggest that the FBA can contribute to adhesion, invasion and spread process of the fungus.Paracoccicoidioides é o agente etiológico da paracoccidioidomicose (PCM), uma doença considerada como primeira causa de mortalidade entre as micoses sistêmicas no Brasil. O sucesso no estabelecimento da infeção está relacionado com a capacidade do fungo de aderir e degradar componentes da matriz extracelular (MEC). O plasminogênio humano (hPlg) é uma proteína presente no plasma, a qual possui atividade fibrinolítica quando é ativado em plasmina. Muitos micro-organismos patogênicos são capazes de subverter o sistema plasminogênio/plasmina através de moléculas ligantes e promovem a degradação de barreiras teciduais. Neste trabalho foram identificadas, através de Far-Western e análise proteômica, um total de 15 proteínas secretadas por Paracoccidioides com habilidade de ligação ao plasminogênio. Essas proteínas são prováveis alvos da interação do patógeno com o hospedeiro, que contribui para o potencial invasivo do fungo. A frutose 1,6-bifosfato aldolase (FBA) foi descrita em outros organismos como ligante de plasminogênio e possui participação na adesão de Paracoccidioides às células do hospedeiro. Selecionamos esta proteína para ensaios de validação e foi observada sua presença na superfície e em vesículas secretoras do fungo. Confirmamos a capacidade da FBA de converter plasminogênio em plasmina na presença do ativador tecidual de plasminogênio (tPA) e essa interação promoveu a degradação de fibrina. Em ensaios de infecção, a adição de anticorpos que bloqueiam o sítio de ligação da FBA reduziu a interação do fungo com macrófagos e a interação de FBA com Plg aumentou o índice de invasão celular. Esses dados sugerem que a FBA pode contribuir no processo de adesão, invasão e disseminação do fungo.Submitted by Erika Demachki (erikademachki@gmail.com) on 2017-02-16T17:00:17Z No. of bitstreams: 2 Dissertação - Edilânia Gomes Araújo Chaves - 2013.pdf: 3289607 bytes, checksum: 174bfb3cce0a9109022321f4adf3368d (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Approved for entry into archive by Erika Demachki (erikademachki@gmail.com) on 2017-02-17T16:53:18Z (GMT) No. of bitstreams: 2 Dissertação - Edilânia Gomes Araújo Chaves - 2013.pdf: 3289607 bytes, checksum: 174bfb3cce0a9109022321f4adf3368d (MD5) license_rdf: 0 bytes, checksum: d41d8cd98f00b204e9800998ecf8427e (MD5)Made available in DSpace on 2017-02-17T16:53:18Z (GMT). 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dc.title.por.fl_str_mv Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
dc.title.alternative.eng.fl_str_mv Identification and analysis of plasminogen binding proteins of Paracoccidioides
title Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
spellingShingle Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
Chaves, Edilânia Gomes Araújo
Paracoccidioides
Proteoma
Secretoma
Plasminogênio
Proteome
Secretome
Plasminogen
CIENCIAS BIOLOGICAS::MICROBIOLOGIA
title_short Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
title_full Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
title_fullStr Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
title_full_unstemmed Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
title_sort Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
author Chaves, Edilânia Gomes Araújo
author_facet Chaves, Edilânia Gomes Araújo
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.referee1.fl_str_mv Bailão, Alexandre Melo
dc.contributor.referee2.fl_str_mv Amaral, André Corrêa
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/1438544283655466
dc.contributor.author.fl_str_mv Chaves, Edilânia Gomes Araújo
contributor_str_mv Soares, Célia Maria de Almeida
Bailão, Alexandre Melo
Amaral, André Corrêa
dc.subject.por.fl_str_mv Paracoccidioides
Proteoma
Secretoma
Plasminogênio
topic Paracoccidioides
Proteoma
Secretoma
Plasminogênio
Proteome
Secretome
Plasminogen
CIENCIAS BIOLOGICAS::MICROBIOLOGIA
dc.subject.eng.fl_str_mv Proteome
Secretome
Plasminogen
dc.subject.cnpq.fl_str_mv CIENCIAS BIOLOGICAS::MICROBIOLOGIA
description Paracoccicoidioides is the etiological agent of paracoccidioidomycosis (PCM), a disease considered one of the main causes of mortality among systemic mycoses in Brazil. The success in establishing of the infection is related with the ability of fungus to adhere and degrade components of the extracellular matrix (ECM). Human plasminogen (hPlg) is a protein of blood plasma of the host that presents fibrinolytic activity when activated into plasmin. Many pathogens are able to subvert the plasminogen/plasmin system using linker molecules and promote the degradation of tissue barriers. In this work, we identified through Far Western and proteomic analysis, a total of 15 proteins secreted of Paracoccidioides that are plasminogen binding proteins. Those proteins are probable targets of the interaction of the fungus with the host and could contribute to the invasiveness of the fungus. The fructose 1,6-biphosphate aldolase was described in other organisms such as plasminogen binder and presentes participation in the adherence of Paracoccidioides to host cells. This protein selected for validation tests and their presence was observed on the surface and secretory vesicles of the fungus. FBA confirm the ability to convert plasminogen to plasmin in the presence of tissue plasminogen activator (tPA) and this interaction promoted the degradation of fibrin. In infection assays, the addition of antibodies blocking the FBA binding site reduced the interaction of the fungus with macrophages and the interaction of FBA with Plg increased the rate of cell invasion. These data suggest that the FBA can contribute to adhesion, invasion and spread process of the fungus.
publishDate 2013
dc.date.issued.fl_str_mv 2013-03-20
dc.date.accessioned.fl_str_mv 2017-02-17T16:53:18Z
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dc.identifier.citation.fl_str_mv CHAVES, E. G. A. Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides. 2013. 59 f. Dissertação (mestrado em Medicina Tropical e Saúde Pública) - Universidade Federal de Goiás, Goiânia, 2013.
dc.identifier.uri.fl_str_mv http://repositorio.bc.ufg.br/tede/handle/tede/6856
identifier_str_mv CHAVES, E. G. A. Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides. 2013. 59 f. Dissertação (mestrado em Medicina Tropical e Saúde Pública) - Universidade Federal de Goiás, Goiânia, 2013.
url http://repositorio.bc.ufg.br/tede/handle/tede/6856
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dc.publisher.initials.fl_str_mv UFG
dc.publisher.country.fl_str_mv Brasil
dc.publisher.department.fl_str_mv Instituto de Patologia Tropical e Saúde Pública - IPTSP (RG)
publisher.none.fl_str_mv Universidade Federal de Goiás
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