ArticlePloS one2014
Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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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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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Galactose-deficient IgA1 and the corresponding IgG autoantibodies predict IgA nephropathy progression.PloS one · 2019Trial
- Ultrasensitive Immunoassay Using a Novel Galactose-Deficient IgA1 Antibody and Its Clinical Application in the Diagnosis of IgAN.Kidney international reports · 2026Article
- Loss of GalNAc-T14 links O-glycosylation defects to alterations in B cell homing in IgA nephropathy.The Journal of clinical investigation · 2025Article
- Benefits and Pitfalls of a Glycosylation Inhibitor Tunicamycin in the Therapeutic Implication of Cancers.Cells · 2024Review
- Racial heterogeneity of IgA1 hinge-regioniScience · 2022Article
- New Insights into the Treatment of Glomerular Diseases: When Mechanisms Become Vivid.International journal of molecular sciences · 2022Review
- Aberrantly Glycosylated IgA1 in IgA Nephropathy: What We Know and What We Don't Know.Journal of clinical medicine · 2021Review
- Quantitative assessment of successive carbohydrate additions to the clustered O-glycosylation sites of IgA1 by glycosyltransferases.Glycobiology · 2021Article
- Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021Article
- Review
- Analysis of O-glycoforms of the IgA1 hinge region by sequential deglycosylation.Scientific reports · 2020Article
- Aberrant Glycosylation of the IgA1 Molecule in IgA Nephropathy.Seminars in nephrology · 2018Review
- Assay for galactose-deficient IgA1 enables mechanistic studies with primary cells from IgA nephropathy patients.BioTechniques · 2018Article
- Comparative Glycomics of Immunoglobulin A and G From Saliva and Plasma Reveals Biomarker Potential.Frontiers in immunology · 2018Article
- Quantitative Age-specific Variability of Plasma Proteins in Healthy Neonates, Children and Adults.Molecular & cellular proteomics : MCP · 2017Article
- Glyco-engineering for the production of recombinant IgA1 with distinct mucin-type O-glycans in plants.Bioengineered · 2016Article
- Potential diagnostic biomarkers for IgA nephropathy: a comparative study pre- and post-tonsillectomy.International urology and nephrology · 2016Article
- The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy.Frontiers in immunology · 2016Review
- N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
12 authors at 3 institutions in 4 countries.
Funding
Abstract
Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed O-glycosylation heterogeneity of naturally asialo-IgA1 (Ale) myeloma protein that mimics Gal-deficient IgA1 (Gd-IgA1) of patients with IgAN, except that IgA1 O-glycans of IgAN patients are frequently sialylated. Specifically, serum IgA1 of healthy controls has more α2,3-sialylated O-glycans (NeuAc attached to Gal) than α2,6-sialylated O-glycans (NeuAc attached to GalNAc). As IgA1-producing cells from IgAN patients have an increased activity of α2,6-sialyltransferase (ST6GalNAc), we hypothesize that such activity may promote premature sialylation of GalNAc and, thus, production of Gd-IgA1, as sialylation of GalNAc prevents subsequent Gal attachment. Distribution of NeuAc in IgA1 O-glycans may play an important role in the pathogenesis of IgAN. To better understand biological functions of NeuAc in IgA1, we established protocols for enzymatic sialylation leading to α2,3- or α2,6-sialylation of IgA1 O-glycans. Sialylation of Gal-deficient asialo-IgA1 (Ale) myeloma protein by an ST6GalNAc enzyme generated sialylated IgA1 that mimics the Gal-deficient IgA1 glycoforms in patients with IgAN, characterized by α2,6-sialylated Gal-deficient GalNAc. In contrast, sialylation of the same myeloma protein by an α2,3-sialyltransferase yielded IgA1 typical for healthy controls, characterized by α2,3-sialylated Gal. The GalNAc-specific lectin from Helix aspersa (HAA) is used to measure levels of Gd-IgA1. We assessed HAA binding to IgA1 sialylated at Gal or GalNAc. As expected, α2,6-sialylation of IgA1 markedly decreased reactivity with HAA. Notably, α2,3-sialylation also decreased reactivity with HAA. Neuraminidase treatment recovered the original HAA reactivity in both instances. These results suggest that binding of a GalNAc-specific lectin is modulated by sialylation of GalNAc as well as Gal in the clustered IgA1 O-glycans. Thus, enzymatic sialylation offers a useful model to test the role of NeuAc in reactivities of the clustered O-glycans with lectins.
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Registered trials
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