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Article Dans Une Revue Cell Reports Année : 2018

Galectin-8 Favors the Presentation of Surface-Tethered Antigens by Stabilizing the B Cell Immune Synapse

Dorian Obino
Odile Malbec
  • Fonction : Auteur
Thibaut Léger
Ana-Maria Lennon-Duménil
  • Fonction : Auteur correspondant

Résumé

Complete activation of B cells relies on their capacity to extract tethered antigens from immune synapses by either exerting mechanical forces or promoting their proteolytic degradation through lysosome secretion. Whether antigen extraction can also be tuned by local cues originating from the lymphoid microenvironment has not been investigated. We here show that the expression of Galectin-8-a glycan-binding protein found in the extracellular milieu, which regulates interactions between cells and matrix proteins-is increased within lymph nodes under inflammatory conditions where it enhances B cell arrest phases upon antigen recognition in vivo and promotes synapse formation during BCR recognition of immobilized antigens. Galectin-8 triggers a faster recruitment and secretion of lysosomes toward the B cell-antigen contact site, resulting in efficient extraction of immobilized antigens through a proteolytic mechanism. Thus, extracellular cues can determine how B cells sense and extract tethered antigens and thereby tune B cell responses in vivo.

Dates et versions

hal-01955896 , version 1 (14-12-2018)

Licence

Paternité - Pas d'utilisation commerciale - Pas de modification

Identifiants

Citer

Dorian Obino, Luc Fetler, Andrea Soza, Odile Malbec, Juan José Saez, et al.. Galectin-8 Favors the Presentation of Surface-Tethered Antigens by Stabilizing the B Cell Immune Synapse. Cell Reports, 2018, 25 (11), pp.3110-3122.e6. ⟨10.1016/j.celrep.2018.11.052⟩. ⟨hal-01955896⟩
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