ArticleNature communications2024
N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Nuclear N-glycosylation maintains H3K9me3 heterochromatin and genomic stability.Nature cell biology · 2026Article
- Site-specific profiling of structure and function of Igµ B cell receptor glycans.Nature communications · 2026Article
- Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025Review
- Fc Proteoforms of ACPA IgG Discriminate Autoimmune Responses in Plasma and Synovial Fluid of Rheumatoid Arthritis Patients and Associate with Disease Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Enzymatic Desialylation Enables Reliable Charge Variant Characterization of Highly Glycosylated and Sialylated Fc Fusion Proteins.ACS pharmacology & translational science · 2025Article
- Non-Glycosylated SARS-CoV-2 Omicron BA.5 Receptor Binding Domain (RBD) with a Native-like Conformation Induces a Robust Immune Response with Potent Neutralization in a Mouse Model.Molecules (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IgG secreted by B cells carry asparagine N(297)-linked glycans in the fragment crystallizable (Fc) region. Changes in Fc glycosylation are related to health or disease and are functionally relevant, as IgG without Fc glycans cannot bind to Fcɣ receptors or complement factors. However, it is currently unknown whether ɣ-heavy chain (ɣHC) glycans also influence the function of membrane-bound IgG-B-cell receptors (BCR) and thus the outcome of the B-cell immune response. Here, we show in a germinal center (GC)-derived human B-cell line that ɣHC glycans do not affect membrane expression of IgG-BCRs. Furthermore, antigen binding or other BCR-facilitated mechanisms appear unaffected, including BCR downmodulation or BCR-mediated signaling. As expected, secreted IgG lacking Fc glycosylation is unable to carry out effector functions. Together, these observations indicate that IgG-Fc glycosylation serves as a mechanism to control the effector functions of antibodies, but does not regulate the activation of IgG-switched B cells, as its absence had no apparent impact on BCR function.
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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.