Evidence for Conformational Mechanism on the Binding of TgMIC4 with β-Galactose-Containing Carbohydrate Ligand

摘要: A deeper understanding of the role sialic/desialylated groups during TgMIC4-glycoproteins interactions has importance to better clarify odd process host cell invasion by members apicomplexan phylum. Within this context, we evaluated interaction established recombinant TgMIC4 (the whole molecule) with sialylated (bovine fetuin) and desialylated (asialofetuin) glycoproteins using functionalized quartz crystal microbalance dissipation monitoring (QCM-D). suitable receptive surface containing for β-galactose-containing carbohydrate ligand (limit quantification ∼ 40 μM) was designed used as biomolecular recognition platform study binding conformational mechanisms glycoprotein (fetuin), or not, terminal sialic group (asialofetuin). It inferred that binding/interaction depends on presence/absence in target protein is possible be differentiated through a slower kinetic step QCM-D approach (which are inferring thus associated β-galactose ligand). This likely supposed (from mechanical energetic analysis obtained measurements) involved Toxoplasma gondii causative agent toxoplasmosis) parasitic accompanied (galactose) induced change (i.e., internalization can additionally dependent structural changes, controlled absence specific galactose), addition TgMIC4-glycoprotein solely process.