ArticleJournal of immunological methods2015
A method for high-throughput, sensitive analysis of IgG Fc and Fab glycosylation by capillary electrophoresis.
Article in Journal of immunological methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 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.
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Who cites it
74 citing papers in PubMed, 107 citations in OpenAlex.
- Adenovectored RSV prefusion glycoprotein + soluble glycoprotein combination immunization establishes persistent opsonophagocytic antibody response through IgG3.Frontiers in immunology · 2025Trial
- Nucleocapsid-specific antibody function is associated with therapeutic benefits from COVID-19 convalescent plasma therapy.Cell reports. Medicine · 2022Trial
- Systems serology identifies FcR-related autoantibody signatures and functions for Sjögren's syndrome.EMBO molecular medicine · 2026Article
- Breast milk antibody Fc signatures track with HIV transmission during breastfeeding in ART-naïve mothers.iScience · 2026Article
- Antigen-specific IgG glycosylation profiles in hamsters and macaques following COVID-19 vaccination.iScience · 2026Article
- Immunoglobulin GFrontiers in immunology · 2026Article
- ESAT-6 and CFP-10 reactive IgG in patients with tuberculosis inhibits intracellular bacteria.Cell reports · 2025Article
- Temporal and Sex-DependentInternational journal of molecular sciences · 2025Article
- Kinetic Modeling of the Antibody Disulfide Bond Reduction Reaction With Integrated Prediction of the Drug Load Profile for Cysteine-Conjugated ADCs.Biotechnology and bioengineering · 2025Article
- Raider of the lostFrontiers in molecular biosciences · 2025Article
- A multivalent binding model infers antibody Fc species from systems serology.PLoS computational biology · 2024Article
- Altered Spike Immunoglobulin G Fc N-Linked Glycans Are Associated With Hyperinflammatory State in Adult Coronavirus Disease 2019 and Multisystem Inflammatory Syndrome in Children.Open forum infectious diseases · 2024Article
- Altered spike IgG Fc N-linked glycans are associated with hyperinflammatory state in adult COVID and Multisystem Inflammatory Syndrome in Children.medRxiv : the preprint server for health sciences · 2024Article
- Antigen specificity shapes antibody functions in tuberculosis.bioRxiv : the preprint server for biology · 2024Article
- Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection.Nature communications · 2024Article
- Diverging Maternal and Cord Antibody Functions From SARS-CoV-2 Infection and Vaccination in Pregnancy.The Journal of infectious diseases · 2024Article
- Immune profiling of SARS-CoV-2 infection during pregnancy reveals NK cell and γδ T cell perturbations.JCI insight · 2023Article
- Robust induction of functional humoral response by a plant-derived Coronavirus-like particle vaccine candidate for COVID-19.NPJ vaccines · 2023Article
- Enhancing the therapeutic activity of hyperimmune IgG against chikungunya virus using FcγRIIIa affinity chromatography.Frontiers in immunology · 2023Article
- Explore how immobilization strategies affected immunosensor performance by comparing four methods for antibody immobilization on electrode surfaces.Scientific reports · 2022Article
14 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 at 4 institutions in 2 countries.
Funding
Abstract
The N-glycan of the IgG constant region (Fc) plays a central role in tuning and directing multiple antibody functions in vivo, including antibody-dependent cellular cytotoxicity, complement deposition, and the regulation of inflammation, among others. However, traditional methods of N-glycan analysis, including HPLC and mass spectrometry, are technically challenging and ill suited to handle the large numbers of low concentration samples analyzed in clinical or animal studies of the N-glycosylation of polyclonal IgG. Here we describe a capillary electrophoresis-based technique to analyze plasma-derived polyclonal IgG-glycosylation quickly and accurately in a cost-effective, sensitive manner that is well suited for high-throughput analyses. Additionally, because a significant fraction of polyclonal IgG is glycosylated on both Fc and Fab domains, we developed an approach to separate and analyze domain-specific glycosylation in polyclonal human, rhesus and mouse IgGs. Overall, this protocol allows for the rapid, accurate, and sensitive analysis of Fc-specific IgG glycosylation, which is critical for population-level studies of how antibody glycosylation may vary in response to vaccination or infection, and across disease states ranging from autoimmunity to cancer in both clinical and animal studies.
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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.