Adhesion of the human pathogen Sporothrix schenckii to several extracellular matrix proteins

The pathogenic fungus Sporothrix schenckii is the causative agent of sporot richosis. This subcutaneous mycosis may disseminate in immunocompromised in dividuals and also affect several internal organs and tissues, most commonl y the bone, joints and lung. Since adhesion is the first step involved with the dissemination of pathogens in the host, we have studied the interactio n between S, schenckii and several extracellular matrix (ECM) proteins. The binding of two morphological phases of S. schenckii, yeast cells and conid ia, to immobilized type II collagen, laminin, fibronectin, fibrinogen and t hrombospondin was investigated. Poly (2-hydroxyethyl methacrylate) (poly-HE MA) was used as the negative control. Cell adhesion was assessed by ELISA w ith a rabbit anti-S. schenckii antiserum. The results indicate that both mo rphological phases of this fungus can bind significantly to type II collage n, fibronectin and laminin in comparison to the binding observed with BSA ( used as blocking agent). The adhesion rate observed with the ECM proteins ( type II collagen, fibronectin and laminin) was statistically significant (P <0.05) when compared to the adhesion obtained with BSA. No significant bind ing of conidia was observed to either fibrinogen or thrombospondin, but yea st cells did bind to the fibrinogen. Our results indicate that S. schenckii can bind to fibronectin, laminin and type II collagen and also show differ ences in binding capacity according to the morphological form of the fungus .