Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

Jeremy Bonzi, Olivier Bornet, Stephane Betzi, Brian T. Kasper, Lara K. Mahal, Stephane J. Mancini, Claudine Schiff, Corinne Sebban-Kreuzer, Francoise Guerlesquin and Latifa Elantak ()
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Jeremy Bonzi: Laboratoire d’Ingénierie des Systèmes Macromoléculaires
Olivier Bornet: Aix-Marseille Université
Stephane Betzi: Aix-Marseille Université
Brian T. Kasper: Biomedical Chemistry Institute, New York University
Lara K. Mahal: Biomedical Chemistry Institute, New York University
Stephane J. Mancini: Aix-Marseille Université
Claudine Schiff: Aix-Marseille Université
Corinne Sebban-Kreuzer: Laboratoire d’Ingénierie des Systèmes Macromoléculaires
Francoise Guerlesquin: Laboratoire d’Ingénierie des Systèmes Macromoléculaires
Latifa Elantak: Laboratoire d’Ingénierie des Systèmes Macromoléculaires

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract Galectins are glycan-binding proteins involved in various biological processes including cell/cell interactions. During B-cell development, bone marrow stromal cells secreting galectin-1 (GAL1) constitute a specific niche for pre-BII cells. Besides binding glycans, GAL1 is also a pre-B cell receptor (pre-BCR) ligand that induces receptor clustering, the first checkpoint of B-cell differentiation. The GAL1/pre-BCR interaction is the first example of a GAL1/unglycosylated protein interaction in the extracellular compartment. Here we show that GAL1/pre-BCR interaction modifies GAL1/glycan affinity and particularly inhibits binding to LacNAc containing epitopes. GAL1/pre-BCR interaction induces local conformational changes in the GAL1 carbohydrate-binding site generating a reduction in GAL1/glycan affinity. This fine tuning of GAL1/glycan interactions may be a strategic mechanism for allowing pre-BCR clustering and pre-BII cells departure from their niche. Altogether, our data suggest a novel mechanism for a cell to modify the equilibrium of the GAL1/glycan lattice involving GAL1/unglycosylated protein interactions.

Date: 2015
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DOI: 10.1038/ncomms7194

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