Interaction of surface molecules on Cryptococcus neoformans with plasminogen

• DOI: 10.1111/1567-1364.12131
• Publication Date: 2013-12-21T00:21:45Z
• Authors: Reiko Ikeda; Tomoe Ichikawa
• Keywords: 0301 basic medicine; 0303 health sciences; Plasminogen; Surface Plasmon Resonance; 3. Good health; Plasminogen Activators; 03 medical and health sciences; Polysaccharides; Cryptococcus neoformans; Humans; Fibrinolysin; Research Articles; Biotransformation; Protein Binding

Microbial pathogens are known to express molecules that interact with host proteins, leading invasion and colonization. For example, some pathogenic microorganisms proteins bind enhance the activity of plasminogen. In this way, utilize fibrinolytic system promote invasion. We found triosephosphate isomerase (TPI), a glycolytic enzyme produced by Staphylococcus aureus, bound mannooligosaccharides from capsulated fungus Cryptococcus neoformans human plasminogen, suggesting TPI is moonlighting protein. Several C. surface thought be plasminogen-binding proteins. Here, we examined ability polymers (including polysaccharides) Heat-killed cells transformed plasminogen into plasmin in dose-dependent manner presence tissue activator. Soluble polysaccharides were based on plasmon resonance (SPR) analysis. Neutral fractionated using DEAE column chromatography activated However, fraction containing glucuronoxylomannan (the primary component capsule) did not activate addition, binding between was weak. Components neutral identified as mannose, galactose, glucose xylose. conclusion, may affect fibrinolysis detected