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

A deeper understanding of the role of sialic/desialylated groups during TgMIC4–glycoproteins interactions has importance to better clarify the odd process of host cell invasion by members of the apicomplexan phylum. Within this context, we evaluated the interaction established by recombinant TgMIC4...

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Veröffentlicht in:Langmuir 2015-11, Vol.31 (44), p.12111-12119
Hauptverfasser: Santos, Adriano, Carvalho, Fernanda C, Roque-Barreira, Maria-Cristina, Zorzetto-Fernandes, André Luiz, Gimenez-Romero, David, Monzó, Isidro, Bueno, Paulo R
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container_end_page 12119
container_issue 44
container_start_page 12111
container_title Langmuir
container_volume 31
creator Santos, Adriano
Carvalho, Fernanda C
Roque-Barreira, Maria-Cristina
Zorzetto-Fernandes, André Luiz
Gimenez-Romero, David
Monzó, Isidro
Bueno, Paulo R
description A deeper understanding of the role of sialic/desialylated groups during TgMIC4–glycoproteins interactions has importance to better clarify the odd process of host cell invasion by members of the apicomplexan phylum. Within this context, we evaluated the interaction established by recombinant TgMIC4 (the whole molecule) with sialylated (bovine fetuin) and desialylated (asialofetuin) glycoproteins by using functionalized quartz crystal microbalance with dissipation monitoring (QCM-D). A suitable receptive surface containing recombinant TgMIC4 for monitoring β-galactose-containing carbohydrate ligand (limit of quantification ∼ 40 μM) was designed and used as biomolecular recognition platform to study the binding and conformational mechanisms of TgMIC4 during the interaction with glycoprotein containing (fetuin), or not, terminal sialic group (asialofetuin). It was inferred that the binding/interaction monitoring depends on the presence/absence of sialic groups in target protein and is possible to be differentiated through a slower binding kinetic step using QCM-D approach (which we are inferring to be thus associated with β-galactose ligand). This slower binding/interaction step is likely supposed (from mechanical energetic analysis obtained in QCM-D measurements) to be involved with Toxoplasma gondii (the causative agent of toxoplasmosis) parasitic invasion accompanied by ligand (galactose) induced binding conformational change (i.e., cell internalization process can be additionally dependent on structural conformational changes, controlled by the absence of sialic groups and to the specific binding with galactose), in addition to TgMIC4-glycoprotein solely recognition binding process.
doi_str_mv 10.1021/acs.langmuir.5b03141
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subjects Adsorption
Carbohydrates - chemistry
Galactose - chemistry
Ligands
Molecular Conformation
Protein Binding
Protozoan Proteins - chemistry
Quartz Crystal Microbalance Techniques
Toxoplasma - chemistry
Toxoplasma gondii
title Evidence for Conformational Mechanism on the Binding of TgMIC4 with β‑Galactose-Containing Carbohydrate Ligand
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