ArticleScientific reports2016
The amyloid fold of Gad m 1 epitopes governs IgE binding.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Insights into Api m 10-Isoforms and Splice Variants: More Than One Major IgE-Binding Epitope.Clinical and translational allergy · 2026Article
- Impurities in amyloid studies: The power of automated model building within a cautionary tale for structural biologists.Protein science : a publication of the Protein Society · 2025Article
- Comparative studies of seafood and reptile α- and β-parvalbumins.Protein science : a publication of the Protein Society · 2024Article
- Linear epitopes of bony fish β-parvalbumins.Frontiers in immunology · 2024Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?Clinical reviews in allergy & immunology · 2022Review
- History of safe exposure and bioinformatic assessment of phosphomannose-isomerase (PMI) for allergenic risk.Transgenic research · 2021Article
- Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteomics-Based Methodologies for the Detection and Quantification of Seafood Allergens.Foods (Basel, Switzerland) · 2020Review
- Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.Journal of Parkinson's disease · 2020Review
- Reconstruction of fish allergenicity from the content and structural traits of the component β-parvalbumin isoforms.Scientific reports · 2019Article
- Abundant fish protein inhibits α-synuclein amyloid formation.Scientific reports · 2018Article
- Amyloid Assembly Endows Gad m 1 with Biomineralization Properties.Biomolecules · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are polymeric structural states formed from locally or totally unfolded protein chains that permit surface reorganizations, stability enhancements and interaction properties that are absent in the precursor monomers. β-Parvalbumin, the major allergen in fish allergy, forms amyloids that are recognized by IgE in the patient sera, suggesting a yet unknown pathological role for these assemblies. We used Gad m 1 as the fish β-parvalbumin model and a combination of approaches, including peptide arrays, recombinant wt and mutant chains, biophysical characterizations, protease digestions, mass spectrometry, dot-blot and ELISA assays to gain insights into the role of amyloids in the IgE interaction. We found that Gad m 1 immunoreactive regions behave as sequence-dependent conformational epitopes that provide a 1000-fold increase in affinity and the structural repetitiveness required for optimal IgE binding and cross-linking upon folding into amyloids. These findings support the amyloid state as a key entity in type I food allergy.
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