ArticleThe Journal of experimental medicine2014
Monovalent engagement of the BCR activates ovalbumin-specific transnuclear B cells.
Article in The Journal of experimental medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 62 citations in OpenAlex.
- Towards a unifying model for B-cell receptor triggering.Nature reviews. Immunology · 2025Review
- Mouse B cells engineered to express an anti-HPV antibody elicit anti-tumor T cell responses.Frontiers in immunology · 2025Article
- Engineered human B cells targeting tumor-associated antigens exhibit antigen presentation and antibody-mediated functions.Frontiers in immunology · 2025Article
- Engineered protein subunit COVID19 vaccine is as immunogenic as nanoparticles in mouse and hamster models.Scientific reports · 2024Article
- Effect of Antigen Valency on Autoreactive B-Cell Targeting.Molecular pharmaceutics · 2024Article
- A universal design of restructured dimer antigens: Development of a superior vaccine against the paramyxovirus in transgenic rice.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Validation of a murine proteome-wide phage display library for identification of autoantibody specificities.JCI insight · 2023Article
- Antigen footprint governs activation of the B cell receptor.Nature communications · 2023Article
- Suppression of allograft rejection by regulatory B cells induced via TLR signaling.JCI insight · 2022Article
- Impact of oligomerization on the allergenicity of allergens.Clinical and molecular allergy : CMA · 2022Review
- Induction of antigen-specific tolerance by nanobody-antigen adducts that target class-II major histocompatibility complexes.Nature biomedical engineering · 2021Article
- Shedding Structured Light on Molecular Immunity: The Past, Present and Future of Immune Cell Super Resolution Microscopy.Frontiers in immunology · 2021Review
- Factors in B cell competition and immunodominance.Immunological reviews · 2020Review
- Regulatory B cells require antigen recognition for effective allograft tolerance induction.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2020Article
- Modular Polymer Antigens To Optimize Immunity.Biomacromolecules · 2019Article
- Programming Structured DNA Assemblies to Probe Biophysical Processes.Annual review of biophysics · 2019Review
- Weak Multivalent Binding of Influenza Hemagglutinin Nanoparticles at a Sialoglycan-Functionalized Supported Lipid Bilayer.ACS nano · 2019Article
- One-Pot Dual Labeling of IgG 1 and Preparation of C-to-C Fusion Proteins Through a Combination of Sortase A and Butelase 1.Bioconjugate chemistry · 2018Article
- Immuno-receptors: from recognition to signaling and function.European biophysics journal : EBJ · 2018Review
- The Coordination Between B Cell Receptor Signaling and the Actin Cytoskeleton During B Cell Activation.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Valency requirements for B cell activation upon antigen encounter are poorly understood. OB1 transnuclear B cells express an IgG1 B cell receptor (BCR) specific for ovalbumin (OVA), the epitope of which can be mimicked using short synthetic peptides to allow antigen-specific engagement of the BCR. By altering length and valency of epitope-bearing synthetic peptides, we examined the properties of ligands required for optimal OB1 B cell activation. Monovalent engagement of the BCR with an epitope-bearing 17-mer synthetic peptide readily activated OB1 B cells. Dimers of the minimal peptide epitope oriented in an N to N configuration were more stimulatory than their C to C counterparts. Although shorter length correlated with less activation, a monomeric 8-mer peptide epitope behaved as a weak agonist that blocked responses to cell-bound peptide antigen, a blockade which could not be reversed by CD40 ligation. The 8-mer not only delivered a suboptimal signal, which blocked subsequent responses to OVA, anti-IgG, and anti-kappa, but also competed for binding with OVA. Our results show that fine-tuning of BCR-ligand recognition can lead to B cell nonresponsiveness, activation, or inhibition.
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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.