Interaction of human fibronectin with Candida glabrata epithelial adhesin 6 (Epa6).

摘要: Adherence of pathogens to extracellular matrix proteins and host cells is one the essential steps in microbial colonization human organism. The adhesion C. glabrata, i.e. second major causative agent disseminated candidiases after albicans, epithelium mainly engages specific fungal cell wall - epithelial adhesins (Epa) particular, Epa1, Epa6 Epa7. aim present study was identify Epa protein involved interactions with fibronectin kinetic thermodynamic characteristics these interactions. A relatively novel gel-free approach, "cell surface shaving" that consists short treatment trypsin employed glabrata surfaceome. purified, isolated characterized terms its affinity using a microplate ligand-binding assay plasmon resonance measurements. dissociation constants for binding were determined range between 9.03 × 10(-9) M 7.22 10(-8) M, depending on method used (surface measurements versus assay, respectively). identified pathogen-human protein-protein might become potential target anticandidal therapeutic approaches.