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 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

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Pre-B Cell Receptors
Galectin 1
carbohydrates
Polysaccharides
affinity
Carbohydrates
interactions
cells
Cell Communication
proteins
bone marrow
compartments
Cluster Analysis
B-Lymphocytes
Cells
Galectins
Biological Phenomena
tuning
ligands

ASJC Scopus subject areas

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

Cite this

Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions. / Bonzi, Jeremy; Bornet, Olivier; Betzi, Stephane; Kasper, Brian T.; Mahal, Lara; Mancini, Stephane J.; Schiff, Claudine; Sebban-Kreuzer, Corinne; Guerlesquin, Francoise; Elantak, Latifa.

In: Nature Communications, Vol. 6, 6194, 25.02.2015.

Research output: Contribution to journalArticle

Bonzi, J, Bornet, O, Betzi, S, Kasper, BT, Mahal, L, Mancini, SJ, 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, vol. 6, 6194. https://doi.org/10.1038/ncomms7194
Bonzi, Jeremy ; Bornet, Olivier ; Betzi, Stephane ; Kasper, Brian T. ; Mahal, Lara ; Mancini, Stephane J. ; Schiff, Claudine ; Sebban-Kreuzer, Corinne ; Guerlesquin, Francoise ; Elantak, Latifa. / Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions. In: Nature Communications. 2015 ; Vol. 6.
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