title: Glycan dependence of Galectin-3 self-association properties.
abstract: Human Galectin-3 is found in the nucleus, the cytoplasm and at the cell surface. This lectin is constituted of two domains: an unfolded N-terminal domain and a C-terminal Carbohydrate Recognition Domain (CRD). There are still uncertainties about the relationship between the quaternary structure of Galectin-3 and its carbohydrate binding properties. Two types of self-association have been described for this lectin: a C-type self-association and a N-type self-association. Herein, we have analyzed Galectin-3 oligomerization by Dynamic Light Scattering using both the recombinant CRD and the full length lectin. Our results proved that LNnT induces N-type self-association of full length Galectin-3. Moreover, from Nuclear Magnetic Resonance (NMR) and Surface Plasmon Resonance experiments, we observed no significant specificity or affinity variations for carbohydrates related to the presence of the N-terminal domain of Galectin-3. NMR mapping clearly established that the N-terminal domain interacts with the CRD. We propose that LNnT induces a release of the N-terminal domain resulting in the glycan-dependent self-association of Galectin-3 through N-terminal domain interactions.
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Moléculaires, UMR 7255, CNRS, Aix-Marseille Université, Marseille, France.
authors.forename: Hubert
authors.initials: H
authors.lastname: Halimi
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Moléculaires, UMR 7255, CNRS, Aix-Marseille Université, Marseille, France; U1006 INSERM, Aix-Marseille Université, Marseille, France.
authors.forename: Annafrancesca
authors.initials: A
authors.lastname: Rigato
authors.affiliation: Institut de la Microbiologie de la Méditerranée, FR 3479, CNRS, Aix-Marseille Université, Marseille, France.
authors.forename: Deborah
authors.initials: D
authors.lastname: Byrne
authors.affiliation: Centre de Recherche en Neurobiologie et Neurophysiologie de Marseille, UMR 7286, Aix-Marseille Université, Marseille, France.
authors.forename: Géraldine
authors.initials: G
authors.lastname: Ferracci
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Moléculaires, UMR 7255, CNRS, Aix-Marseille Université, Marseille, France.
authors.forename: Corinne
authors.initials: C
authors.lastname: Sebban-Kreuzer
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Moléculaires, UMR 7255, CNRS, Aix-Marseille Université, Marseille, France.
authors.forename: Latifa
authors.initials: L
authors.lastname: ElAntak
authors.affiliation: Laboratoire d'Ingénierie des Systèmes Moléculaires, UMR 7255, CNRS, Aix-Marseille Université, Marseille, France.
authors.forename: Francoise
authors.initials: F
authors.lastname: Guerlesquin
mesh_terms: D001798:Blood Proteins; D037502:Galectin 3 / Q000737:chemistry*; D037161:Galectins; D006031:Glycosylation; D006801:Humans; D007785:Lactose / Q000737:chemistry; D008958:Models, Molecular; D009844:Oligosaccharides / Q000737:chemistry; D011485:Protein Binding; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D020836:Protein Structure, Quaternary
chemical_list: D001798:Blood Proteins; D037502:Galectin 3; D037161:Galectins; C428445:LGALS3 protein, human; D009844:Oligosaccharides; C013084:lacto-N-neotetraose; D007785:Lactose