ArticleThe Journal of biological chemistry2015
Unmasking of CD22 Co-receptor on Germinal Center B-cells Occurs by Alternative Mechanisms in Mouse and Man.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 65 citations in OpenAlex.
- Interpretable and scalable spatial gene set activity analysis with GESSO uncovers functional tissue architecture.bioRxiv : the preprint server for biology · 2026Article
- Siglec-G on B cells restrains the germinal center response by controlling T cell help during positive selection.bioRxiv : the preprint server for biology · 2026Article
- An atlas of human siglecs integrates expression, affinity, and cis/trans sialoglycan recognition profiles.Nature communications · 2026Article
- Sialic acids modulate immune responses in cancer: Therapeutic opportunities.The Journal of biological chemistry · 2026Review
- Spatial multi-omics integration by cross-modal graph contrastive learning.Briefings in bioinformatics · 2026Article
- An ultrasensitive and modular platform to detect Siglec ligands and control immune cell function.Science advances · 2025Article
- Modeling glycans with AlphaFold 3: capabilities, caveats, and limitations.Glycobiology · 2025Article
- M2-Like Macrophages Exhibit Sialic Acid-Enhanced Efferocytosis via the Siglec CD22.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Understanding the Glycosylation Pathways Involved in the Biosynthesis of the Sulfated Glycan Ligands for Siglecs.ACS chemical biology · 2025Article
- CD21Frontiers in immunology · 2025Article
- The forecasting power of the mucin-microbiome interplay in livestock respiratory diseases.The veterinary quarterly · 2024Article
- Chemoenzymatic Synthesis of SulfatedJACS Au · 2024Article
- Sialic acid in the regulation of blood cell production, differentiation and turnover.Immunology · 2024Review
- Dissecting the abilities of murine Siglecs to interact with gangliosides.The Journal of biological chemistry · 2024Article
- GL7 ligand expression defines a novel subset of CD4Mucosal immunology · 2023Article
- Glycome dynamics in T and B cell development: basic immunological mechanisms and clinical applications.Trends in immunology · 2023Review
- Absolute Affinities from Quantitative Shotgun Glycomics Using Concentration-Independent (COIN) Native Mass Spectrometry.ACS central science · 2023Article
- The role ofFrontiers in immunology · 2023Review
- Role of tumor cell sialylation in pancreatic cancer progression.Advances in cancer research · 2023Review
- Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
CD22 is an inhibitory B-cell co-receptor whose function is modulated by sialic acid (Sia)-bearing glycan ligands. Glycan remodeling in the germinal center (GC) alters CD22 ligands, with as yet no ascribed biological consequence. Here, we show in both mice and humans that loss of high affinity ligands on GC B-cells unmasks the binding site of CD22 relative to naive and memory B-cells, promoting recognition of trans ligands. The conserved modulation of CD22 ligands on GC B-cells is striking because high affinity glycan ligands of CD22 are species-specific. In both species, the high affinity ligand is based on the sequence Siaα2-6Galβ1-4GlcNAc, which terminates N-glycans. The human ligand has N-acetylneuraminic acid (Neu5Ac) as the sialic acid, and the high affinity ligand on naive B-cells contains 6-O-sulfate on the GlcNAc. On human GC B-cells, this sulfate modification is lost, giving rise to lower affinity CD22 ligands. Ligands of CD22 on naive murine B-cells do not contain the 6-O-sulfate modification. Instead, the high affinity ligand for mouse CD22 has N-glycolylneuraminic acid (Neu5Gc) as the sialic acid, which is replaced on GC B-cells with Neu5Ac. Human naive and memory B-cells express sulfated glycans as high affinity CD22 ligands, which are lost on GC B-cells. In mice, Neu5Gc-containing glycans serve as high affinity CD22 ligands that are replaced by Neu5Ac-containing glycans on GC B-cells. Our results demonstrate that loss of high affinity CD22 ligands on GC B-cells occurs in both mice and humans through alternative mechanisms, unmasking CD22 relative to naive and memory B-cells.
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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.