Differentially expressed proteins in Paracoccidioides brasiliensis involved in extracellular matrix adhesion

In this work we proposed to verify the protein profile expressed and the ligand to extracellular matrix components (ECM) by Paracoccidioides brasiliensis (Pb) isolates because the understanding and identification of these molecules it's very important in the discovery of efficient treatments for the systemic mycoses. All the isolates of Pb presented different capacity to adhere to epithelial cells. Pb protein extracts were analyzed by two‐dimensional electrophoresis and ligand assays showed differential profiles among four isolates: 62 for collagen type I, 18 laminin and 23 fibronectin of a total of 420 proteins observed. So, we identify some proteins by LC‐MS/MS and a frutose 1–6 biphosphate aldolase, 39kDa, pI 6.6, fibronectin ligand was present in 3 of 4 isolates and it might be an anchorless protein involved in Pb adhesion. Using the same approach, we have also isolated an adhesin of 30kDa, that binding to laminin and it was characterized as a 14‐3‐3 protein and this protein involved in a wide range of vital regulatory processes, such as mitogenic signal transduction, apoptotic cell death and cell cycle control. Expressive number of proteins, with characteristics of ECM ligands, was observed mainly in the isolates more virulent, showing the potential of this fungal in the interaction host parasite. Supported by CAPES, FAPESP, FINEP and PADC‐FCF.