Identificação e análise de proteínas ligantes de plasminogênio de Paracoccidioides
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2013-03-20
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Universidade Federal de Goiás
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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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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.