ArticleMolecular & cellular proteomics : MCP2015
Hinge-Region O-Glycosylation of Human Immunoglobulin G3 (IgG3).
Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03394092 (Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis), which is not on this map. Cited by 66 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis
Who cites it
66 citing papers in PubMed.
- Hinge-region Cys-to-Ser mutation enables homogeneous DAR6 anti-c-Met biparatopic ADCs with tolerable O-glycosylation.Antibody therapeutics · 2026Article
- Orthodox vs. Paradox: Supporting the Central Dogma With Sugar Code.Proteomics · 2026Review
- Polyclonal Antibody Therapeutics: Analytical Innovations and Regulatory Perspectives for Addressing Heterogeneity Challenges.Analytical chemistry · 2026Review
- Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026Review
- IgG N-glycosylation in autoimmune diseases.Frontiers in immunology · 2026Review
- Widespread Fab-arm exchange affects all endogenous serum IgG4.Nature communications · 2025Article
- Discovery and Characterization of Unusual O-Linked Glycosylation of IgG4 Antibody Using LC-MS.Rapid communications in mass spectrometry : RCM · 2025Article
- A First Insight into the Developability of an Immunoglobulin G3: A Combined Computational and Experimental Approach.ACS pharmacology & translational science · 2024Article
- The genetics and epidemiology of N- and O-immunoglobulin A glycomics.Genome medicine · 2024Article
- Immunoglobulin G glycosylation and its alterations in aging-related diseases.Acta biochimica et biophysica Sinica · 2024Review
- Engineering Agonistic Bispecifics to Investigate the Influence of Distance on Surface-Mediated Complement Activation.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line.Nature communications · 2024Article
- IgG1 versus IgG3: influence of antibody-specificity and allotypic variance on virus neutralization efficacy.Frontiers in immunology · 2024Article
- Are Changes in Serum IgG Glycosylation Related to the Severe Course of SARS-CoV-2 Infection and Recovery Process? In Search of New Diagnostic and Prognostic Biomarkers.Journal of inflammation research · 2024Article
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Complement is activated by elevated IgG3 hexameric platforms and deposits C4b onto distinct antibody domains.Nature communications · 2023Article
- Altered glycosylation profiles of serum IgG in Takayasu arteritis.European journal of medical research · 2023Article
- Article
- Impact of structural modifications of IgG antibodies on effector functions.Frontiers in immunology · 2023Review
- Antibody class-switching as a strategy to improve HIV-1 neutralization.Trends in molecular medicine · 2022Review
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin G (IgG) is one of the most abundant proteins present in human serum and a fundamental component of the immune system. IgG3 represents ∼8% of the total amount of IgG in human serum and stands out from the other IgG subclasses because of its elongated hinge region and enhanced effector functions. This study reports partial O-glycosylation of the IgG3 hinge region, observed with nanoLC-ESI-IT-MS(/MS) analysis after proteolytic digestion. The repeat regions within the IgG3 hinge were found to be in part O-glycosylated at the threonine in the triple repeat motif. Non-, mono- and disialylated core 1-type O-glycans were detected in various IgG3 samples, both poly- and monoclonal. NanoLC-ESI-IT-MS/MS with electron transfer dissociation fragmentation and CE-MS/MS with CID fragmentation were used to determine the site of IgG3 O-glycosylation. The O-glycosylation site was further confirmed by the recombinant production of mutant IgG3 in which potential O-glycosylation sites had been knocked out. For IgG3 samples from six donors we found similar O-glycan structures and site occupancies, whereas for the same samples the conserved N-glycosylation of the Fc CH2 domain showed considerable interindividual variation. The occupancy of each of the three O-glycosylation sites was found to be ∼10% in six serum-derived IgG3 samples and ∼13% in two monoclonal IgG3 allotypes.
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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.