ArticleGlycobiology2017
Siglec-8 and Siglec-9 binding specificities and endogenous airway ligand distributions and properties.
Article in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 130 citations in OpenAlex.
- Acquisition of specific human respiratory tract binding by 2.3.4.4b H5N1 hemagglutinins requires multiple mutations.Journal of virology · 2026Article
- Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells.Nature communications · 2026Article
- Airway mucins function as endogenous inhibitors of neutrophil extracellular traps.bioRxiv : the preprint server for biology · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Establishment and validation of an alternative automated synthesis of [68Ga]Ga-DOTA-Siglec-9 in an independent laboratory for clinical use.EJNMMI radiopharmacy and chemistry · 2025Article
- Characterization of M11-like and OC125-like Monoclonal Antibody Binding to CA125 Tandem Repeats.Biosensors · 2025Article
- Simple and accessible methods for quantifying isolated mucins for further evaluation.MethodsX · 2025Article
- Review
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Understanding the Glycosylation Pathways Involved in the Biosynthesis of the Sulfated Glycan Ligands for Siglecs.ACS chemical biology · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- Eosinophils in inflammatory bowel disease pathogenesis: an ROS-centric view.Frontiers in allergy · 2025Article
- Comprehensive Modular Synthesis of Ganglioside Glycans and Evaluation of their Binding Affinities to Siglec-7 and Siglec-9.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the human esophagus.Glycobiology · 2024Article
- Chemoenzymatic Synthesis of SulfatedJACS Au · 2024Article
- Quantifying Siglec-sialylated ligand interactions: a versatileChemical science · 2024Article
- Dissecting the abilities of murine Siglecs to interact with gangliosides.The Journal of biological chemistry · 2024Article
- RNA Sequencing of Whole Blood in Premature Coronary Artery Disease: Identification of Novel Biomarkers and Involvement of T Cell Imbalance.Journal of cardiovascular translational research · 2024Article
- Unraveling Molecular Recognition of Glycan Ligands by Siglec-9 via NMR Spectroscopy and Molecular Dynamics Modeling.ACS chemical biology · 2024Article
- Intratumoral Influenza Vaccine Administration Attenuates Breast Cancer Growth and Restructures the Tumor Microenvironment through Sialic Acid Binding of Vaccine Hemagglutinin.International journal of molecular sciences · 2023Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Siglecs are transmembrane sialoglycan binding proteins, most of which are expressed on leukocyte subsets and have inhibitory motifs that translate cell surface ligation into immune suppression. In humans, Siglec-8 on eosinophils, mast cells and basophils and Siglec-9 on neutrophils, monocytes and some T-cells, mediate immune cell death, inhibition of immune mediator release and/or enhancement of anti-inflammatory mediator release. Endogenous sialoglycan ligands in tissues, mostly uncharacterized, engage siglecs on leukocytes to inhibit inflammation. Glycan array analyses demonstrated that Siglec-8, Siglec-9 and their mouse counterparts Siglec-F and Siglec-E (respectively) have distinct glycan binding specificities, with Siglec-8 more structurally restricted. Since siglecs are involved in lung inflammation, we studied Siglec-8 and Siglec-9 ligands in human lungs and airways. Siglec-8 ligands are in tracheal submucosal glands and cartilage but not airway epithelium or connective tissues, whereas Siglec-9 ligands are broadly distributed. Mouse airways do not have Siglec-8 ligands, whereas Siglec-9 ligands are on airways of both species. Extraction of human airways and lung followed by electrophoretic resolution and siglec blotting revealed Siglec-8 ligands in extracts of human trachea and cultured tracheal gland cells, but not parenchyma or cultured airway epithelial cells whereas Siglec-9 ligands were extracted from all airway and lung tissues and cells tested. Siglec-8 and Siglec-9 ligands in airways appear to be high molecular weight O-linked sialoglycoproteins. These data reveal differential glycan specificities of Siglec-8, Siglec-9 and their mouse counterparts Siglec-F and Siglec-E, and the tissue distributions and molecular characteristics of Siglec-8 and Siglec-9 sialoglycan ligands on human airways and lungs.
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Registered trials
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.