Ultrasensitive carbohydrate-peptide SPR imaging microarray for diagnosing IgE mediated peanut allergy

Joshi, Amit; Peczuh, Mark W.; Kumar, Challa V.; Rusling, James F.

doi:10.1039/c4an01544d

Cited by 25 publications

(12 citation statements)

References 32 publications

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“…Finally, a surface plasmon resonance imaging microarray has been developed for peanut allergen, Ara h 2, which measures both peptide and carbohydrate epitopes. This method uses magnetic beads coated with anti-IgE monoclonal antibody to capture IgE, is highly sensitive (0.5 pg/ml), and can be completed in 45 min [23•]. Further studies are needed to investigate whether surface plasmon resonance technology can be used for other allergens.…”

Section: Next-generation Innovationsmentioning

confidence: 99%

Technological Innovations for High-Throughput Approaches to In Vitro Allergy Diagnosis

Chapman

Wuenschmann

King

et al. 2015

Curr Allergy Asthma Rep

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Allergy diagnostics is being transformed by the advent of in vitro IgE testing using purified allergen molecules, combined with multiplex technology and biosensors, to deliver discriminating, sensitive, and high-throughput molecular diagnostics at the point of care. Essential elements of IgE molecular diagnostics are purified natural or recombinant allergens with defined purity and IgE reactivity, planar or bead-based multiplex systems to enable IgE to multiple allergens to be measured simultaneously, and, most recently, nanotechnology-based biosensors that facilitate rapid reaction rates and delivery of test results via mobile devices. Molecular diagnostics relies on measurement of IgE to purified allergens, the “active ingredients” of allergenic extracts. Typically, this involves measuring IgE to multiple allergens which is facilitated by multiplex technology and biosensors. The technology differentiates between clinically significant cross-reactive allergens (which could not be deduced by conventional IgE assays using allergenic extracts) and provides better diagnostic outcomes. Purified allergens are manufactured under good laboratory practice and validated using protein chemistry, mass spectrometry, and IgE antibody binding. Recently, multiple allergens (from dog) were expressed as a single molecule with high diagnostic efficacy. Challenges faced by molecular allergy diagnostic companies include generation of large panels of purified allergens with known diagnostic efficacy, access to flexible and robust array or sensor technology, and, importantly, access to well-defined serum panels form allergic patients for product development and validation. Innovations in IgE molecular diagnostics are rapidly being brought to market and will strengthen allergy testing at the point of care.

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Section: Next-generation Innovationsmentioning

confidence: 99%

Technological Innovations for High-Throughput Approaches to In Vitro Allergy Diagnosis

Chapman

Wuenschmann

King

et al. 2015

Curr Allergy Asthma Rep

View full text Add to dashboard Cite

show abstract

“…Joshi et al. reported on an ultrasensitive carbohydrate–peptide surface plasmon resonance imaging microarray in which they immobilized peptide and xylosyl glycoside of Ara h 2 onto carboxylated gold slides and amplified the response with 1‐micrometer‐diameter magnetic beads coated with ˜60,000 polyclonal anti‐IgE molecules. These proof‐of‐concept microarrays that have used novel imaging systems and allergen extracts bound to chips raise theoretical concerns about the analytical sensitivity of the assays and whether the limited binding capacity of microdot surface on an activated glass chip can immobilize sufficient molar concentrations of allergen (especially from allergen extracts) to quantitatively bind IgE antibody in the presence of other antibody isotypes. Alternative multiplex technologies are capable of detecting IgE antibody in human serum.…”

Section: Current Assay Technologymentioning

confidence: 99%

EAACI Molecular Allergology User's Guide

Matricardi

Kleine-Tebbe²,

Hoffmann

et al. 2016

Pediatric Allergy Immunology

724

870

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The availability of allergen molecules ('components') from several protein families has advanced our understanding of immunoglobulin E (IgE)-mediated responses and enabled 'component-resolved diagnosis' (CRD). The European Academy of Allergy and Clinical Immunology (EAACI) Molecular Allergology User's Guide (MAUG) provides comprehensive information on important allergens and describes the diagnostic options using CRD. Part A of the EAACI MAUG introduces allergen molecules, families, composition of extracts, databases, and diagnostic IgE, skin, and basophil tests. Singleplex and multiplex IgE assays with components improve both sensitivity for low-abundance allergens and analytical specificity; IgE to individual allergens can yield information on clinical risks and distinguish cross-reactivity from true primary sensitization. Part B discusses the clinical and molecular aspects of IgE-mediated allergies to foods (including nuts, seeds, legumes, fruits, vegetables, cereal grains, milk, egg, meat, fish, and shellfish), inhalants (pollen, mold spores, mites, and animal dander), and Hymenoptera venom. Diagnostic algorithms and short case histories provide useful information for the clinical workup of allergic individuals targeted for CRD. Part C covers protein families containing ubiquitous, highly cross-reactive panallergens from plant (lipid transfer proteins, polcalcins, PR-10, profilins) and animal sources (lipocalins, parvalbumins, serum albumins, tropomyosins) and explains their diagnostic and clinical utility. Part D lists 100 important allergen molecules. In conclusion, IgE-mediated reactions and allergic diseases, including allergic rhinoconjunctivitis, asthma, food reactions, and insect sting reactions, are discussed from a novel molecular perspective. The EAACI MAUG documents the rapid progression of molecular allergology from basic research to its integration into clinical practice, a quantum leap in the management of allergic patients.

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“…More recently, we reported the first immunoarray for IgE antibodies utilizing both peptide and carbohydrate epitopes. However, the measured concentrations of IgE antibodies that bound to each epitope were statistically indistinguishable . In this study, we have modified the experimental design to improve the selectivity of IgE antibody binding to different epitopes.…”

Section: Methodsmentioning

confidence: 99%

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

et al. 2018

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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 Immuno-CAP assays and the new SPRi method.

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Ultrasensitive carbohydrate-peptide SPR imaging microarray for diagnosing IgE mediated peanut allergy

Cited by 25 publications

References 32 publications

Technological Innovations for High-Throughput Approaches to In Vitro Allergy Diagnosis

Technological Innovations for High-Throughput Approaches to In Vitro Allergy Diagnosis

EAACI Molecular Allergology User's Guide

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

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