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, Latifa Elantak

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Article number6194
JournalNature communications
Volume6
DOIs
StatePublished - Feb 25 2015

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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    Bonzi, J., Bornet, O., Betzi, S., Kasper, B. T., Mahal, L. K., Mancini, S. J., Schiff, C., Sebban-Kreuzer, C., Guerlesquin, F., & Elantak, L. (2015). Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions. Nature communications, 6, [6194]. https://doi.org/10.1038/ncomms7194