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© K. Melican.
Human microvessel (red) colonized by N. meningitidis (green).
Publication : Cell reports

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cell reports - 11 Dec 2018

Obino D, Fetler L, Soza A, Malbec O, Saez JJ, Labarca M, Oyanadel C, Del Valle Batalla F, Goles N, Chikina A, Lankar D, Segovia-Miranda F, Garcia C, Léger T, Gonzalez A, Espéli M, Lennon-Duménil AM, Yuseff MI

Link to Pubmed [PMID] – 30540943

Cell Rep 2018 Dec;25(11):3110-3122.e6

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.

https://www.ncbi.nlm.nih.gov/pubmed/30540943