Análise proteômica da parede celular de leveduras de Paracoccidioides americana e Paracoccidioides brasiliensis

Abstract

Paracoccidioidomycosis (PCM) is the most important systemic mycosis in Latin America. PCM is endemic in Brazil; however, it is not mandatory to report, so its actual incidence and prevalence are unknown. The etiologic agents of PCM are dimorphic fungi of the genus Paracoccidioides, which in the human host transits from mycelial to yeast cells. The cell wall is the most superficial structure of the fungus and, therefore, is important during the infection stage. The cell wall is a dynamic structure that undergoes constant remodeling, to ensure pathogen adaptation to multiple stress conditions within the human host. In addition, the cell wall also plays an important role in the processes of cell division, growth, and transition, therefore, and due to the absence of this structure in human cells, the cell wall becomes an interesting target for study. The aim of the present work was to perform proteomic study of cell wall proteins that are covalently linked by disulfide bridges, in two representative species of the genus Paracoccidioides, Paracoccidioides americana and Paracoccidioides brasiliensis. Proteomic analysis allowed the identification of differentially expressed proteins between the two species. Proteins associated with the adhesion to extracellular matrix components such as enolase, GAPDH, 14-3-3 family proteins, and proteins that bind and activate plasminogen such as enolase, fructose-1, 6-biphosphate aldolase 1 and phosphoglycerate kinase were more expressed in the P. brasiliensis cell wall. In addition, heat shock response proteins such as Hsp90 co-chaperone AHA1 and Hsp STI1 were more expressed on the cell wall of P. brasiliensis; while, catalase P was more expressed in P. americana. These results can help to understand the host-parasite relationship and guide the selection of proteins that can serve as new pharmacological targets.