Skip to Main content Skip to Navigation
Journal articles

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

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.
Complete list of metadata

Cited literature [54 references]  Display  Hide  Download

https://hal.archives-ouvertes.fr/hal-02018118
Contributor : Latifa Elantak Connect in order to contact the contributor
Submitted on : Wednesday, February 13, 2019 - 3:59:25 PM
Last modification on : Monday, July 12, 2021 - 9:39:10 AM
Long-term archiving on: : Tuesday, May 14, 2019 - 7:06:48 PM

File

ncomms7194.pdf
Publisher files allowed on an open archive

Identifiers

Collections

Citation

Jeremy Bonzi, Olivier Bornet, Stéphane Betzi, Brian Kasper, Lara Mahal, et al.. Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions. Nature Communications, Nature Publishing Group, 2015, 6 (1), pp.6194. ⟨10.1038/ncomms7194⟩. ⟨hal-02018118⟩

Share

Metrics

Record views

106

Files downloads

263