ArticleThe Journal of allergy and clinical immunology2016
Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen.
Article in The Journal of allergy and clinical immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 77 citations in OpenAlex.
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- The optimized endolysosomal degradation assay with standardized enzyme activity represents an orthogonal method for predicting protein immunogenicity and T cell epitopes.Frontiers in allergy · 2026Article
- Mucosal vaccination with enzymatically activeFrontiers in microbiology · 2026Article
- Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues.Scientific reports · 2024Article
- Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?Frontiers in allergy · 2024Review
- NLRP3 promotes allergic responses to birch pollen extract in a model of intranasal sensitization.Frontiers in immunology · 2024Article
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- Editorial: The regulation of allergic responses by proteolysis: from protease allergens to host proteases modulation.Frontiers in allergy · 2024Article
- 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
- Structural Framework for Analysis of CD4+ T-Cell Epitope Dominance in Viral Fusion Proteins.Biochemistry · 2023Review
- Structure and IgE Cross-Reactivity among Cashew, Pistachio, Walnut, and Peanut Vicilin-Buried Peptides.Journal of agricultural and food chemistry · 2023Article
- Mechanistic insights into silica nanoparticle-allergen interactions on antigen presenting cell function in the context of allergic reactions.Nanoscale · 2023Article
- CD4+ T-Cell Epitope Prediction by Combined Analysis of Antigen Conformational Flexibility and Peptide-MHCII Binding Affinity.Biochemistry · 2022Article
- Development of a Liquid Chromatography and High-Resolution and -Accuracy Mass Spectrometry Method to Evaluate New Biotherapeutic Entity Processing in Human Liver Lysosomes.ImmunoHorizons · 2022Article
- Surface Functionalization of Silica Nanoparticles: Strategies to Optimize the Immune-Activating Profile of Carrier Platforms.Pharmaceutics · 2022Article
- Bet v 1 and other birch allergens are more resistant to proteolysis and more abundant than other birch pollen proteins.Allergy · 2022Article
- Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides.Journal of agricultural and food chemistry · 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
- pH-dependent structural diversity of profilin allergens determines thermal stability.Frontiers in allergy · 2022Article
Corrections and comments
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Authors and funding
24 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundThe search for intrinsic factors, which account for a protein's capability to act as an allergen, is ongoing. Fold stability has been identified as a molecular feature that affects processing and presentation, thereby influencing an antigen's immunologic properties.
objectiveWe assessed how changes in fold stability modulate the immunogenicity and sensitization capacity of the major birch pollen allergen Bet v 1.
methodsBy exploiting an exhaustive virtual mutation screening, we generated mutants of the prototype allergen Bet v 1 with enhanced thermal and chemical stability and rigidity. Structural changes were analyzed by means of x-ray crystallography, nuclear magnetic resonance, and molecular dynamics simulations. Stability was monitored by using differential scanning calorimetry, circular dichroism, and Fourier transform infrared spectroscopy. Endolysosomal degradation was simulated in vitro by using the microsomal fraction of JAWS II cells, followed by liquid chromatography coupled to mass spectrometry. Immunologic properties were characterized in vitro by using a human T-cell line specific for the immunodominant epitope of Bet v 1 and in vivo in an adjuvant-free BALB/c mouse model.
resultsFold stabilization of Bet v 1 was pH dependent and resulted in resistance to endosomal degradation at a pH of 5 or greater, affecting presentation of the immunodominant T-cell epitope in vitro. These properties translated in vivo into a strong allergy-promoting TH2-type immune response. Efficient TH2 cell activation required both an increased stability at the pH of the early endosome and efficient degradation at lower pH in the late endosomal/lysosomal compartment.
conclusionsOur data indicate that differential pH-dependent fold stability along endosomal maturation is an essential protein-inherent determinant of allergenicity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.