ArticleThe Journal of experimental medicine2015
A single glycan on IgE is indispensable for initiation of anaphylaxis.
Article in The Journal of experimental medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 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.
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Who cites it
89 citing papers in PubMed, 148 citations in OpenAlex.
- LeGenD: High-throughput N-glycan profiling using explainable AI and lectin profiling.The Journal of biological chemistry · 2026Article
- Pairing of high-mannose glycans in human IgE-Fc: implications for secretion and stability.Clinical proteomics · 2026Article
- A Case for Anti-IgE Vaccination.Allergy · 2026Review
- Mpi-driven N-glycosylation orchestrates mucin O-glycosylation and intestinal homeostasis.Nature communications · 2026Article
- Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026Review
- IgE based therapeutics are an emerging modality in cancer treatment.Discover oncology · 2025Review
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- Vaccine-Induced Anti-IgE Antibodies Neutralize Free IgE but Fail to Bind and Activate Mast Cell-Displayed IgE.Allergy · 2025Article
- Aberrant Activation of Mast Cells: Molecular Mechanisms and Targets for Intervention.Clinical reviews in allergy & immunology · 2025Review
- Glycosylation as an intricate post-translational modification process takes part in glycoproteins related immunity.Cell communication and signaling : CCS · 2025Review
- Maternal IgE Influence on Fetal and Infant Health.Immunological reviews · 2025Review
- Pathogenic and Nonpathogenic Antibody Responses in Allergic Diseases.European journal of immunology · 2025Review
- LuLIPLEX: A Fast, Highly Sensitive, and Multiplexed Method for the Detection of IgE Against Major Allergens.Allergy · 2025Article
- Engrafted NSG-SGM3 humanized mice spontaneously produce human immunoglobulins including IgE.Frontiers in immunology · 2025Article
- The role of immunoglobulin E in non-atopic disorders.Frontiers in immunology · 2025Review
- Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025Review
- The multifaceted potential ofHeliyon · 2024Review
- Whence and wherefore IgE?Immunological reviews · 2024Review
- A Comparison of Natural and Therapeutic Anti-IgE Antibodies.Antibodies (Basel, Switzerland) · 2024Review
- Elevated level of multibranched complex glycan reveals an allergic tolerance status.Clinical proteomics · 2024Article
29 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 5 institutions in 2 countries.
Funding
Abstract
Immunoglobulin ε (IgE) antibodies are the primary mediators of allergic diseases, which affect more than 1 in 10 individuals worldwide. IgE specific for innocuous environmental antigens, or allergens, binds and sensitizes tissue-resident mast cells expressing the high-affinity IgE receptor, FcεRI. Subsequent allergen exposure cross-links mast cell-bound IgE, resulting in the release of inflammatory mediators and initiation of the allergic cascade. It is well established that precise glycosylation patterns exert profound effects on the biological activity of IgG. However, the contribution of glycosylation to IgE biology is less clear. Here, we demonstrate an absolute requirement for IgE glycosylation in allergic reactions. The obligatory glycan was mapped to a single N-linked oligomannose structure in the constant domain 3 (Cε3) of IgE, at asparagine-394 (N394) in human IgE and N384 in mouse. Genetic disruption of the site or enzymatic removal of the oligomannose glycan altered IgE secondary structure and abrogated IgE binding to FcεRI, rendering IgE incapable of eliciting mast cell degranulation, thereby preventing anaphylaxis. These results underscore an unappreciated and essential requirement of glycosylation in IgE biology.
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What OpenQuestion holds
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.