ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 87 citations in OpenAlex.
- Predictions from deep learning propose substantial protein-carbohydrate interplay.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- An atlas of human siglecs integrates expression, affinity, and cis/trans sialoglycan recognition profiles.Nature communications · 2026Article
- Writers and readers of sialylation in immunoregulation in cancer.The Journal of biological chemistry · 2026Review
- An ultrasensitive and modular platform to detect Siglec ligands and control immune cell function.Science advances · 2025Article
- Understanding the Glycosylation Pathways Involved in the Biosynthesis of the Sulfated Glycan Ligands for Siglecs.ACS chemical biology · 2025Article
- Tools for structural lectinomics: From structures to lectomes.BBA advances · 2025Article
- Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands.Journal of the American Chemical Society · 2024Article
- Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the human esophagus.Glycobiology · 2024Article
- Targeting Siglec-Sialylated MUC1 Immune Axis in Cancer.Cancers · 2024Review
- GlcNAc6ST2/CHST4 Is Essential for the Synthesis of R-10G-Reactive Keratan Sulfate/SulfatedMolecules (Basel, Switzerland) · 2024Article
- Siglecs as potential targets of therapy in human mast cell- and/or eosinophil-associated diseases.Seminars in immunology · 2023Review
- Human sialoglycan ligands for immune inhibitory Siglecs.Molecular aspects of medicine · 2023Review
- Siglecs in allergy and asthma.Molecular aspects of medicine · 2023Review
- Drug delivery targets and strategies to address mast cell diseases.Expert opinion on drug delivery · 2023Review
- Article
- Structures of the Inhibitory Receptor Siglec-8 in Complex with a High-Affinity Sialoside Analogue and a Therapeutic Antibody.JACS Au · 2023Article
- Interactions between Siglec-8 and endogenous sialylated cis ligands restrain cell death induction in human eosinophils and mast cells.Frontiers in immunology · 2023Article
- Sequence variety in the CC' loop of Siglec-8/9/3 determines the recognitions to sulfated oligosaccharides.Computational and structural biotechnology journal · 2023Article
- Computationally guided conversion of the specificity of E-selectin to mimic that of Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Complementary Role of GlcNAc6ST2 and GlcNAc6ST3 in Synthesis of CL40-Reactive Sialylated and Sulfated Glycans in the Mouse Pleural Mesothelium.Molecules (Basel, Switzerland) · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Siglec-8 is a human immune-inhibitory receptor that, when engaged by specific self-glycans, triggers eosinophil apoptosis and inhibits mast cell degranulation, providing an endogenous mechanism to down-regulate immune responses of these central inflammatory effector cells. Here we used solution NMR spectroscopy to dissect the fine specificity of Siglec-8 toward different sialylated and sulfated carbohydrate ligands and determined the structure of the Siglec-8 lectin domain in complex with its prime glycan target 6'-sulfo sialyl Lewis(x) A canonical motif for sialic acid recognition, extended by a secondary motif formed by unique loop regions, recognizing 6-O-sulfated galactose dictates tight specificity distinct from other Siglec family members and any other endogenous glycan recognition receptors. Structure-guided mutagenesis revealed key contacts of both interfaces to be equally essential for binding. Our work provides critical structural and mechanistic insights into how Siglec-8 selectively recognizes its glycan target, rationalizes the functional impact of site-specific glycan sulfation in modulating this lectin-glycan interaction, and will enable the rational design of Siglec-8-targeted agonists to treat eosinophil- and mast cell-related allergic and inflammatory diseases, such as asthma.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.