ArticlePloS one2017
Antibodies Targeting Closely Adjacent or Minimally Overlapping Epitopes Can Displace One Another.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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
21 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Structural and Functional Insights Into IgE Receptor Interactions and Disruptive Inhibition.Immunological reviews · 2025Review
- Competitive Epitope Binning Using HT-SPR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Epitope binning for multiple antibodies simultaneously using mammalian cell display and DNA sequencing.Communications biology · 2024Article
- Deep serological profiling of the Trypanosoma cruzi TSSA antigen reveals different epitopes and modes of recognition by Chagas disease patients.PLoS neglected tropical diseases · 2023Article
- Potent monoclonal antibodies neutralize Omicron sublineages and other SARS-CoV-2 variants.Cell reports · 2022Article
- Moving beyond Titers.Vaccines · 2022Review
- Computational epitope binning reveals functional equivalence of sequence-divergent paratopes.Computational and structural biotechnology journal · 2022Article
- Directed evolution of and structural insights into antibody-mediated disruption of a stable receptor-ligand complex.Nature communications · 2021Article
- Anti-NKG2D single domain-based antibodies for the modulation of anti-tumor immune response.Oncoimmunology · 2020Article
- A highly potent CD73 biparatopic antibody blocks organization of the enzyme active site through dual mechanisms.The Journal of biological chemistry · 2020Article
- Characterizing Epitope Binding Regions of Entire Antibody Panels by Combining Experimental and Computational Analysis of Antibody: Antigen Binding Competition.Molecules (Basel, Switzerland) · 2020Article
- Efficient elimination of primary B-ALL cells in vitro and in vivo using a novel 4-1BB-based CAR targeting a membrane-distal CD22 epitope.Journal for immunotherapy of cancer · 2020Article
- Assessing the binding properties of the anti-PD-1 antibody landscape using label-free biosensors.PloS one · 2020Article
- Article
- Rapid Antibody Selection Using Surface Plasmon Resonance for High-Speed and Sensitive Hazelnut Lateral Flow Prototypes.Biosensors · 2018Article
- Article
- Single-Domain Antibodies and the Promise of Modular Targeting in Cancer Imaging and Treatment.Frontiers in immunology · 2018Review
- Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here we describe how real-time label-free biosensors can be used to identify antibodies that compete for closely adjacent or minimally overlapping epitopes on their specific antigen via a mechanism of antibody displacement. By kinetically perturbing one another's binding towards their antigen via the formation of a transient trimolecular complex, antibodies can displace one another in a fully reversible and dose-dependent manner. Displacements can be readily identified when epitope binning assays are performed in a classical sandwich assay format whereby a solution antibody (analyte) is tested for binding to its antigen that is first captured via an immobilized antibody (ligand) because an inverted sandwiching response is observed when an analyte displaces a ligand, signifying the antigen's unusually rapid dissociation from its ligand. In addition to classifying antibodies within a panel in terms of their ability to block or sandwich pair with one another, displacement provides a hybrid mechanism of competition. Using high-throughput epitope binning studies we demonstrate that displacements can be observed on any target, if the antibody panel contains appropriate epitope diversity. Unidirectional displacements occurring between disparate-affinity antibodies can generate apparent asymmetries in a cross-blocking experiment, confounding their interpretation. However, examining competition across a wide enough concentration range will often reveal that these displacements are reversible. Displacement provides a gentle and efficient way of eluting antigen from an otherwise high affinity binding partner which can be leveraged in designing reagents or therapeutic antibodies with unique properties.
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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.