RESUMO
Trichosporon asahii is the major causative agent of deep-seated trichosporonosis. The virulence factors of this yeast pathogen remain uncharacterized. To investigate the pathogenicity of T. asahii, we focused on the interactions between surface molecules of the yeast and host biomolecules. We examined the ability of surface molecules to bind human plasminogen using clinical isolates of T. asahii. Living T. asahii cells accelerated the conversion of plasminogen to plasmin in a dose-dependent manner in the presence of tissue plasminogen activator. Extracts from cells using lithium chloride contained plasminogen-binding molecules based on surface plasmon resonance (SPR) analyses. In all strains tested, several of the fractions obtained using DEAE column chromatography bound and accelerated the conversion of plasminogen to plasmin. Based on far-Western blotting analyses, a common protein was identified within the four strains, which was identified as a hypothetical protein from genome analyses of T. asahii. blast searches suggested the protein might be heparinase, and heparinase activity was detected in the T. asahii extract. Furthermore, affinity chromatography using plasminogen as a ligand detected one protein band by SDS-PAGE, which was identified as thioredoxin-dependent peroxide reductase.SPR analyses suggested the presence of molecules on T. asahii cells that could bind plasminogen with differing affinities.