ArticleStructure (London, England : 1993)2018
Structural and Dynamic Properties of Allergen and Non-Allergen Forms of Tropomyosin.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 50 citations in OpenAlex.
- Structural Basis for Trivalent Cross-Linking of a Patient-Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201.Allergy · 2026Article
- Mouse Models of Food Allergies: Where Do They Take Us?Clinical reviews in allergy & immunology · 2026Review
- Protein Sequencing with Single Amino Acid Resolution Discerns Peptides That Discriminate Tropomyosin Proteoforms.Journal of proteome research · 2025Article
- An Overview of Seafood Allergens: Structure-Allergenicity Relationship and Allergenicity Elimination Processing Techniques.Foods (Basel, Switzerland) · 2025Review
- Conformational Flexibility of a Lipocalin Allergen (Mus m 1): Implications for Molecular Allergy Diagnostics.Current issues in molecular biology · 2025Article
- To stay or not to stay intact as an allergen: the endolysosomal degradation assay used as tool to analyze protein immunogenicity andFrontiers in allergy · 2024Review
- IgE-Mediated Shellfish Allergy in Children.Nutrients · 2023Review
- Recombinant Tropomyosin from the Pacific Oyster (Foods (Basel, Switzerland) · 2022Article
- Scientific Opinion on development needs for the allergenicity and protein safety assessment of food and feed products derived from biotechnology.EFSA journal. European Food Safety Authority · 2022Article
- Molecular and allergenic characterization of recombinant tropomyosin from mud crab Scylla olivacea.Molecular biology reports · 2021Article
- Article
- Fish Allergy Around the World-Precise Diagnosis to Facilitate Patient Management.Frontiers in allergy · 2021Review
- Statement onEFSA journal. European Food Safety Authority · 2021Article
- Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin.Allergy · 2020Article
- Homologous tropomyosins from vertebrate and invertebrate: Recombinant calibrator proteins in functional biological assays for tropomyosin allergenicity assessment of novel animal foods.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To what extent do structural and biophysical features of food allergen proteins distinguish them from other proteins in our diet? Invertebrate tropomyosins (Tpms) as a class are considered "pan-allergens," inducing food allergy to shellfish and respiratory allergy to dust mites. Vertebrate Tpms are not known to elicit allergy or cross-reactivity, despite their high structural similarity and sequence identity to invertebrate homologs. We expect allergens are sufficiently stable against gastrointestinal proteases to survive for immune sensitization in the intestines, and that proteolytic stability will correlate with thermodynamic stability. Thermal denaturation of shrimp Tpm shows that it is more stable than non-allergen vertebrate Tpm. Shrimp Tpm is also more resistant to digestion. Molecular dynamics uncover local dynamics that select epitopes and global differences in flexibility between shrimp and pig Tpm that discriminate allergens from non-allergens. Molecular determinants of allergenicity depend not only on sequence but on contributions of protein structure and dynamics.
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