Análise do secretoma de duas espécies filogenéticas de Paracoccidioides

• Autor(a) principal: Oliveira, Amanda Rodrigues de
• Data de Publicação: 2015
• Tipo de documento: Dissertação
• Idioma: por
• Título da fonte: Repositório Institucional da UFG
• Texto Completo: http://repositorio.bc.ufg.br/tede/handle/tede/4945
• topic: Paracoccidioides; Proteoma; Adesão; Virulência; Paracoccidioides; Proteome; Adhesion; Virulence; CIENCIAS BIOLOGICAS::GENETICA; BIOQUIMICA::BIOLOGIA MOLECULAR

Paracoccidioides is a termodimorphic fungus that causes paracoccidioidomycosis (PCM), the most frequent systemic mycosis that affects mainly the rural population in Latin America. The fungus grows as yeast when grown at 35-37° C and as mycelium at temperatures below 28° C. The establishment and severity of the disease depends on factors inherent to the fungus and the host. The diversity presented among isolates of the same genus has been explored between the microorganisms and attempt to clarify differences possibly related to virulence existing between isolates that cause the same disease. The secretion of proteins in a cell is a highly dynamic mechanism and is directly involved in the first pathogen contact with the host cells, enabling their survival, multiplication and dissemination. In order to try to elucidate this diversity the proteomic profile of secretome of two isolates of Paracoccidioides, PbEpm83 and Pb01, that in our experimental conditions of infection showed different behaviors was characterized. The use of Ultra Performance liquid chromatography coupled to mass spectrometry (UPLC-MSE) allowed the identification of 92 proteins / isoforms among the strains. Of the 92 proteins identified, 36 were preferentially secreted in PbEpm83 and 35 preferentially secreted in Pb01. Among the identified we can highlight proteins related to various biological processes: adhesion to the ECM, proteins related to thermal and oxidative stress, cell rescue, defense and virulence, proteins with immunogenic capacity, proteins related to defense against antifungal, heat shock proteins, among others. Our analysis showed that most of the proteins identified using non-conventional secretory pathways. Among the identified proteins there are already related proteins as virulence factors, such as, ATP synthase, mitochondrial Peroxiredoxin PRX 1, fructose bisphosphate aldolase, Didpeptidil peptidase, Thioredoxin, TCTP, Hsp70 and Hsp88. Our results highlight the importance of secreted proteins in the establishment of infection and that these species, within the same genus, maintain differences in the levels of protein expression that may reflect their behavior in the success of the infection.