ArticleBiomolecules2020
Impact of Different Lipid Ligands on the Stability and IgE-Binding Capacity of the Lentil Allergen Len c 3.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Lipid ligand binding and membrane interactions of a novel food-derived lipid transfer protein enhance basophil allergic responses.Scientific reports · 2026Article
- Structural and Stability Analysis of GRP Family Allergens Pru p 7 and Cry j 7, Which Cause Pollen and Food Allergy Syndrome.Biomolecules · 2025Article
- 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
- Malnutrition and Allergies: Tipping the Immune Balance towards Health.Journal of clinical medicine · 2024Review
- Structural and Immunological Features of PR-10 Allergens: Focusing on the Major Alder Pollen Allergen Aln g 1.International journal of molecular sciences · 2024Article
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Lentil allergens identification and quantification: An update from omics perspective.Food chemistry. Molecular sciences · 2022Review
- The Role of Lipids in Allergic Sensitization: A Systematic Review.Frontiers in molecular biosciences · 2022Article
- Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3.Membranes · 2021Article
- Do Lipids Influence Gastrointestinal Processing: A Case Study of Major Soybean Allergen Gly m 4.Membranes · 2021Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- Abundance and Stability as Common Properties of Allergens.Frontiers in allergy · 2021Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Previously, we isolated the lentil allergen Len c 3, belonging to the class of lipid transfer proteins, cross-reacting with the major peach allergen Pru p 3 and binding lipid ligands. In this work, the allergenic capacity of Len c 3 and effects of different lipid ligands on the protein stability and IgE-binding capacity were investigated. Impacts of pH and heat treating on ligand binding with Len c 3 were also studied. It was shown that the recombinant Len c 3 (rLen c 3) IgE-binding capacity is sensitive to heating and simulating of gastroduodenal digestion. While being heated or digested, the protein showed a considerably lower capacity to bind specific IgE in sera of allergic patients. The presence of lipid ligands increased the thermostability and resistance of rLen c 3 to digestion, but the level of these effects was dependent upon the ligand's nature. The anionic lysolipid LPPG showed the most pronounced protective effect which correlated well with experimental data on ligand binding. Thus, the Len c 3 stability and allergenic capacity can be retained in the conditions of food heat cooking and gastroduodenal digestion due to the presence of certain lipid ligands.
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