ArticleScientific reports2019
Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specific lipid transfer protein from walnut.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- A Review of Walnut Allergy: Allergens Characteristic, the Impact of Processing on Allergenicity and Future Perspectives.Foods (Basel, Switzerland) · 2026Review
- Lipid ligand binding and membrane interactions of a novel food-derived lipid transfer protein enhance basophil allergic responses.Scientific reports · 2026Article
- Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.Allergy · 2026Article
- IgE-mediated lipid transfer protein allergy in children.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2025Review
- Long-chain fatty acids block allergic reaction against lipid transfer protein Sola l 7 from tomato seeds.Protein science : a publication of the Protein Society · 2024Article
- Article
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Review
- NLRP3 priming due to skin damage precedes LTP allergic sensitization in a mouse model.Scientific reports · 2022Article
- IgE epitopes of Ara h 9, Jug r 3, and Pru p 3 in peanut-allergic individuals from Spain and the US.Frontiers in allergy · 2022Article
- The Role of Lipids in Allergic Sensitization: A Systematic Review.Frontiers in molecular biosciences · 2022Article
- Mammalian derived lipocalin and secretoglobin respiratory allergens strongly bind ligands with potentially immune modulating properties.Frontiers in allergy · 2022Article
- Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3.Membranes · 2021Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- Non-specific lipid-transfer proteins: Allergen structure and function, cross-reactivity, sensitization, and epidemiology.Clinical and translational allergy · 2021Article
- Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens.Journal of visualized experiments : JoVE · 2021Article
- Identification and Physicochemical Characterization of a New Allergen fromInternational journal of molecular sciences · 2020Article
- Impact of Different Lipid Ligands on the Stability and IgE-Binding Capacity of the Lentil Allergen Len c 3.Biomolecules · 2020Article
- Structural characterization and in vitro lipid binding studies of non-specific lipid transfer protein 1 (nsLTP1) from fennel (Foeniculum vulgare) seeds.Scientific reports · 2020Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant non-specific lipid transfer proteins type 1 (nsLTP1) are small basic proteins with a hydrophobic cavity able to host a number of different ligands: i.e. fatty acids, fatty acyl-CoA, phospholipids, glycolipids, and hydroxylated fatty acids. However, ligand binding specificity differs among nsLTPs. Within this protein family, Jug r 3 from walnut has been identified as a major allergen. So far, data on the structural characterization of Jug r 3 and its lipid binding capacity are lacking. We report the results from a fluorescence-based ligand-binding assay and ligand-based NMR experiments, to study the binding interactions between Jug r 3 and the 18-carbon monounsaturated oleic acid. Furthermore, protein-based NMR experiments were employed to detect the oleate binding site of Jug r 3. The NMR data were used to dock the oleate molecule into the structural model of Jug r 3. Finally, the impact of the interaction on the allergenic potential of Jug r 3 was investigated by IgE ELISA with 6 sera from walnut allergic patients. Our data corroborate the hypothesis of direct impact of food-derived matrix on the IgE reactivity of nsLTPs.
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