Influência de ferro na composição de proteínas de superfície não covalentemente ligadas de paracoccidioides brasiliensis

Detalhes bibliográficos
Ano de defesa: 2011
Autor(a) principal: Philippsen, Hellen Kempfer lattes
Orientador(a): Soares, Célia Maria de Almeida lattes
Banca de defesa: Soares, Célia Maria de Almeida, Kipnis, André, Pereira, Maristela, Bailão, Alexandre Melo, Borges, Clayton Luís
Tipo de documento: Dissertação
Tipo de acesso: Acesso aberto
Idioma: por
Instituição de defesa: Universidade Federal de Goiás
Programa de Pós-Graduação: Programa de Pós-graduação em Medicina Tropical e Saúde Publica (IPTSP)
Departamento: Instituto de Patologia Tropical e Saúde Pública - IPTSP (RG)
País: Brasil
Palavras-chave em Português:
Palavras-chave em Inglês:
Área do conhecimento CNPq:
Link de acesso: http://repositorio.bc.ufg.br/tede/handle/tede/3222
Resumo: Paracoccidioides brasiliensis is a dimorphic fungus, the causative agent of paracoccidioidomycosis (PCM), a systemic mycosis that affects mainly people from Latin America. In order to establish infection, many factors are required for P. brasiliensis, such as cell wall remodeling and the ability to capture nutrients from the host. As iron is an important cofactor of many reactions, the host reduces the availability of free iron ions to the pathogen. Therefore, this study aims to elucidate the proteomic profile of the cell wall in response to iron depletion. The extraction of surface proteins of the cell wall in iron restriction and iron replete conditions was performed and the proteomic profile was obtained by two-dimensional electrophoresis with subsequent analysis of images. Statistical analysis demonstrated proteins with differential level of expression in each condition, which were subjected to tryptic digestion and identification by mass spectrometry. It was identified 26 proteins by peptide mass fingerprint (PMF) and/or ions fragmentation (MS/MS). The majority of these proteins have post - translational modifications and only some have in their sequences signal peptide, suggesting that they are addressed to the surface by non-classical pathways.