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

Author

Listed:
  • Jeremy Bonzi

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires
    Aix-Marseille Université)

  • Olivier Bornet

    (Aix-Marseille Université
    Institut de Microbiologie de la Méditerranée)

  • Stephane Betzi

    (Aix-Marseille Université
    Centre de Recherche en Cancérologie de Marseille, Institut Paoli-Calmettes)

  • Brian T. Kasper

    (Biomedical Chemistry Institute, New York University)

  • Lara K. Mahal

    (Biomedical Chemistry Institute, New York University)

  • Stephane J. Mancini

    (Aix-Marseille Université
    Centre d’Immunologie de Marseille-Luminy, Faculté des Sciences de Luminy)

  • Claudine Schiff

    (Aix-Marseille Université
    Centre d’Immunologie de Marseille-Luminy, Faculté des Sciences de Luminy)

  • Corinne Sebban-Kreuzer

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires
    Aix-Marseille Université)

  • Francoise Guerlesquin

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires
    Aix-Marseille Université)

  • Latifa Elantak

    (Laboratoire d’Ingénierie des Systèmes Macromoléculaires
    Aix-Marseille Université)

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.

Suggested Citation

  • Jeremy Bonzi & Olivier Bornet & Stephane Betzi & Brian T. Kasper & Lara K. Mahal & Stephane J. Mancini & Claudine Schiff & Corinne Sebban-Kreuzer & Francoise Guerlesquin & Latifa Elantak, 2015. "Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions," Nature Communications, Nature, vol. 6(1), pages 1-12, May.
  • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7194
    DOI: 10.1038/ncomms7194
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