Journal
CELL REPORTS
Volume 25, Issue 11, Pages 3110-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.11.052
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Funding
- Ecole Doctorale BioSPC
- Universite Paris Diderot
- Universite Paris Descartes
- Fondation pour la Recherche Medicale [FDT20150532056]
- Region Ile-de-France (SESAME)
- Paris-Diderot University (ARS)
- CNRS
- Laboratory of Excellence in Research on Medication and Innovative Therapeutics (LabEx LERMIT) - ANR under the program Investissements d'Avenir [ANR-10-LABX-33]
- ANR @RAction starting grant [ANR-14-ACHN-000]
- FONDECYT [1141182]
- Association Nationale pour la Recherche [ANR-PoLyBex-12-BSV3-0014-001]
- European Research Council [ERC-Strapacemi-GA 243103]
- ECOS [C12S02]
- CONICYT Basal Financial Program [AFB-170005]
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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.
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