ArticleAllergy2019
Multiple roles of Bet v 1 ligands in allergen stabilization and modulation of endosomal protease activity.
Article in Allergy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 64 citations in OpenAlex.
- Multi-country IgE reactivity determination of isoforms of theFrontiers in immunology · 2026Article
- Evaluation of Inhibitory Activity of Novel Monoclonal Antibodies Against Cat Allergen Fel d 7 and Their Application to Analyse Allergen Extracts.Scandinavian journal of immunology · 2025Article
- Structural and Stability Analysis of GRP Family Allergens Pru p 7 and Cry j 7, Which Cause Pollen and Food Allergy Syndrome.Biomolecules · 2025Article
- The Octadecanoids: Synthesis and Bioactivity of 18-Carbon Oxygenated Fatty Acids in Mammals, Bacteria, and Fungi.Chemical reviews · 2025Review
- Can Physicochemical Properties Alter the Potency of Aeroallergens? Part 2 - Impact of Physicochemical Properties.Current allergy and asthma reports · 2024Review
- Article
- Production and Release of Proinflammatory Mediators by the Cockroach Allergen Bla g 1 via a Shared Membrane-Destabilization Mechanism.Biochemistry · 2024Article
- Structural and Immunological Features of PR-10 Allergens: Focusing on the Major Alder Pollen Allergen Aln g 1.International journal of molecular sciences · 2024Article
- Identification, Characterization, Cloning, and Cross-Reactivity of Zan b 2, a Novel Pepper Allergen of 11S Legumin.Journal of agricultural and food chemistry · 2024Article
- Ferroptotic alveolar epithelial type II cells drive TCell death discovery · 2024Article
- Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?Frontiers in allergy · 2024Review
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- The History and Science of the Major Birch Pollen Allergen Bet v 1.Biomolecules · 2023Review
- A novel rubber tree PR-10 protein involved in host-defense response against the white root rot fungus Rigidoporus microporus.BMC plant biology · 2023Article
- 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
- When the allergy alarm bells toll: The role of Toll-like receptors in allergic diseases and treatment.Frontiers in molecular biosciences · 2023Review
- Fluorescence signal of proteins in birch pollen distorted within its native matrix: Identification of the fluorescence suppressor quercetin-3-O-sophoroside.Analytical and bioanalytical chemistry · 2022Article
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Gibberellin-regulated proteins: Emergent allergens.Frontiers in allergy · 2022Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 4 countries.
Funding
Abstract
backgroundOver 100 million people worldwide suffer from birch pollen allergy. Bet v 1 has been identified as the major birch pollen allergen. However, the molecular mechanisms of birch allergic sensitization, including the roles of Bet v 1 and other components of the birch pollen extract, remain incompletely understood. Here, we examined how known birch pollen-derived molecules influence the endolysosomal processing of Bet v 1, thereby shaping its allergenicity.
methodsWe analyzed the biochemical and immunological interaction of ligands with Bet v 1. We then investigated the proteolytic processing of Bet v 1 by endosomal extracts in the presence and absence of ligands, followed by a detailed kinetic analysis of Bet v 1 processing by individual endolysosomal proteases as well as the T-cell epitope presentation in BMDCs.
resultsWe identified E
conclusionBet v 1 can serve as a transporter of pollen-derived, bioactive compounds. When carried to the endolysosome, such compounds can modulate the proteolytic activity, including its processing by cysteine cathepsins. We unveil a paradigm shift from an allergen-centered view to a more systemic view that includes the host endolysosomal enzymes.
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Registered trials
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.