ArticleJournal of leukocyte biology2025
The interaction of Galectin-8 C-terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells.
Article in Journal of leukocyte biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Galectin-9 binding to HLA-DR in dendritic cells controls immune synapse formation and T cell proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Endogenous Galectin-8 protects against Th17 infiltration and fibrosis following acute kidney injury.Molecular medicine (Cambridge, Mass.) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Galectins constitute a family of soluble lectins with unique capacity to induce macroscale rearrangements upon interacting with cell membrane glycoconjugates. Galectin-8 is acknowledged for its role in facilitating antigen uptake and processing upon engaging with cell surface glycoconjugates on antigen-presenting cells. Galectin-8 consists of two covalently fused N- and C-terminal carbohydrate recognition domains, each exhibiting distinct glycan specificity. In this study, we utilized single N- and C-carbohydrate recognition domains recombinant proteins to dissect the nature of Galectin-8-glycan interactions during antigen internalization enhancement. Single C-carbohydrate recognition domain was able to replicate the effect of full-length Galectin-8 on antigen internalization in bone marrow-derived dendritic cells. Antigen uptake enhancement was diminished in the presence of lactose or when N-glycosylation-deficient macrophages served as antigen-presenting cells, underscoring the significance of glycan recognition. Measurement of the elastic modulus using Atomic Force Microscopy unveiled that full-length Galectin-8- and C-carbohydrate recognition domain-stimulated macrophages exhibited heightened membrane stiffness compared to untreated cells, providing a plausible mechanism for their involvement in endocytosis. C-carbohydrate recognition domain proved to be as efficient as full-length Galectin-8 in promoting antigen degradation, suggesting its implication in antigen-processing induction. Lastly, C-carbohydrate recognition domain was able to replicate full-length Galectin-8-induced antigen presentation in the major histocompatibility complex class II (MHC-II) context both in vitro and in vivo. Our findings support the notion that Galectin-8 binds through its C-carbohydrate recognition domain to cell surface N-glycans, thereby altering membrane mechanical forces conducive to soluble antigen endocytosis, processing, and presentation to cognate CD4 T cells. These findings contribute to a deeper comprehension of Galectin-8 and its mechanisms of action, paving the way for the development of more efficacious immunotherapies.
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Registered trials
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