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Epitope-Resolved Detection of Peanut-Specific IgE Antibodies by Surface Plasmon Resonance Imaging.


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 ?-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??L each) in a 45?min assay. Excellent correlation of Ara?h2-specific IgE values was found between ImmunoCAP assays and the new SPRi method.

SUBMITTER: Shen M 

PROVIDER: S-EPMC5965296 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Epitope-Resolved Detection of Peanut-Specific IgE Antibodies by Surface Plasmon Resonance Imaging.

Shen Min M   Joshi Amit A AA   Vannam Raghu R   Dixit Chandra K CK   Hamilton Robert G RG   Kumar Challa V CV   Rusling James F JF   Peczuh Mark W MW  

Chembiochem : a European journal of chemical biology 20180104 3


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 S  ...[more]

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