ArticleJournal of proteome research2012
Naturally occurring structural isomers in serum IgA1 o-glycosylation.
Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 76 citations in OpenAlex.
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Single Molecule Kinetic Fingerprinting of Glycans on IgA1 Antibodies.Analytical chemistry · 2025Article
- Post-Translational Modifications in Multiple Myeloma: Mechanisms of Drug Resistance and Therapeutic Opportunities.Biomolecules · 2025Review
- AsymmetricJournal of the American Chemical Society · 2024Article
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
- Pathogenesis of IgA nephropathy: Omics data inform glycomedicine.Nephrology (Carlton, Vic.) · 2024Article
- Immune abnormalities in IgA nephropathy.Clinical kidney journal · 2023Review
- Racial heterogeneity of IgA1 hinge-regioniScience · 2022Article
- Development and Evaluation of a Robust Sandwich Immunoassay System Detecting Serum WFA-Reactive IgA1 for Diagnosis of IgA Nephropathy.International journal of molecular sciences · 2022Article
- IgA Nephropathy: A Chinese Perspective.Glomerular diseases · 2022Review
- Advances in IgA glycosylation and its correlation with diseases.Frontiers in chemistry · 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
- Alternative Complement Pathway Is Activated and Associated with Galactose-Deficient IgAFrontiers in immunology · 2021Article
- A Direct MS-Based Approach to Profile Human Milk Secretory Immunoglobulin A (IgA1) Reveals Donor-Specific Clonal Repertoires With High Longitudinal Stability.Frontiers in immunology · 2021Article
- Mass spectrometry for the identification and analysis of highly complex glycosylation of therapeutic or pathogenic proteins.Expert review of proteomics · 2020Review
- Analysis of O-glycoforms of the IgA1 hinge region by sequential deglycosylation.Scientific reports · 2020Article
- IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2.Glycobiology · 2019Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
IgA is the most abundantly produced antibody and plays an important role in the mucosal immune system. Human IgA is represented by two isotypes, IgA1 and IgA2. The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain. Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment. The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined. We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein. Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers). These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1. Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue. These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
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