ArticleChembiochem : a European journal of chemical biology2018
Epitope-Resolved Detection of Peanut-Specific IgE Antibodies by Surface Plasmon Resonance Imaging.
Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Sustainable Integration of Nanobiosensors in Biomedical and Civil Engineering: A Comprehensive Review.ACS omega · 2025Review
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- Emerging Biosensors to Detect Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2): A Review.Biosensors · 2021Review
- Multiplexed Immunosensors and Immunoarrays.Analytical chemistry · 2020Review
- E-DNA scaffold sensors and the reagentless, single-step, measurement of HIV-diagnostic antibodies in human serum.Microsystems & nanoengineering · 2020Article
- Restricted Proteolysis and LC-MS/MS To Evaluate the Orientation of Surface-Immobilized Antibodies.Analytical chemistry · 2019Article
- Recent Advances in Surface Plasmon Resonance Imaging Sensors.Sensors (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Peanut allergy can be life-threatening and is mediated by allergen-specific immunoglobulin E (IgE) antibodies. Investigation of IgE antibody binding to allergenic epitopes can identify specific interactions underlying the allergic response. Here, we report a surface plasmon resonance imaging (SPRi) immunoassay for differentiating IgE antibodies by epitope-resolved detection. IgE antibodies were first captured by magnetic beads bearing IgE ϵ-chain-specific antibodies and then introduced into an SPRi array immobilized with epitopes from the major peanut allergen glycoprotein Arachis hypogaea h2 (Ara h2). Differential epitope responses were achieved by establishing a binding environment that minimized cross-reactivity while maximizing analytical sensitivity. IgE antibody binding to each Ara h2 epitope was distinguished and quantified from patient serum samples (10 μL each) in a 45 min assay. Excellent correlation of Ara h2-specific IgE values was found between ImmunoCAP assays and the new SPRi method.
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Registered trials
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