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Analysis of the Ligand Recognition Specificities of Human Ficolins Using Surface Plasmon Resonance

Abstract : Ficolins are innate immune recognition proteins involved in activation of the lectin complement pathway. These oligomeric lectin-like proteins are assembled from subunits consisting of a collagen-like triple helix and a trimeric fibrinogen-like recognition domain. In humans, three ficolins coexist: they differ in their ligand binding specificities, but share the capacity to associate with proteases through their collagen-like stalks and trigger complement activation. We describe methods to decipher the recognition specificities of ficolins, based on surface plasmon resonance, an optical technique allowing real-time and label-free monitoring of biomolecular interactions. This technique was mainly used to characterize and compare binding of the three recombinant full-length ficolins and of their isolated recognition domains to various immobilized BSA-glycoconjugates, acetylated BSA or biotinylated heparin. The avidity phenomenon that enhances the apparent affinity of interactions between oligomeric lectin-like proteins and the multivalent ligands is also discussed.
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https://hal.univ-grenoble-alpes.fr/hal-03200980
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Submitted on : Monday, April 19, 2021 - 5:06:32 PM
Last modification on : Tuesday, October 19, 2021 - 11:20:59 AM
Long-term archiving on: : Tuesday, July 20, 2021 - 7:20:03 PM

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Nicole Thielens, Evelyne Gout, Monique Lacroix, Jean-Baptiste Reiser, Christine Gaboriaud. Analysis of the Ligand Recognition Specificities of Human Ficolins Using Surface Plasmon Resonance. Methods in Molecular Biology, Humana Press/Springer Imprint, 2021, The Complement System. Innovative Diagnostic and Research Protocols, 2227, pp.205-226. ⟨10.1007/978-1-0716-1016-9_19⟩. ⟨hal-03200980⟩

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