ArticleFrontiers in allergy2023
Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7.
Article in Frontiers in allergy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Sensitization to Dog Dander Allergen Can f 1 is Associated with Asthma Symptom Severity and Exacerbations in a Singapore-Malaysia Cohort.Journal of asthma and allergy · 2026Article
- Human IgE monoclonal antibodies define two unusual epitopes trapping dog allergen Can f 1 in different conformations.Protein science : a publication of the Protein Society · 2025Article
- 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
- Malnutrition and Allergies: Tipping the Immune Balance towards Health.Journal of clinical medicine · 2024Review
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Introduction: Pet lipocalins are respiratory allergens with a central hydrophobic ligand-binding cavity called a calyx. Molecules carried in the calyx by allergens are suggested to influence allergenicity, but little is known about the native ligands. Methods: To provide more information on prospective ligands, we report crystal structures, NMR, molecular dynamics, and florescence studies of a dog lipocalin allergen Can f 1 and its closely related (and cross-reactive) cat allergen Fel d 7. Results: Structural comparisons with reported lipocalins revealed that Can f 1 and Fel d 7 calyxes are open and positively charged while other dog lipocalin allergens are closed and negatively charged. We screened fatty acids as surrogate ligands, and found that Can f 1 and Fel d 7 bind multiple ligands with preferences for palmitic acid (16:0) among saturated fatty acids and oleic acid (18:1 cis-9) among unsaturated ones. NMR analysis of methyl probes reveals that conformational changes occur upon binding of pinolenic acid inside the calyx. Molecular dynamics simulation shows that the carboxylic group of fatty acids shuttles between two positively charged amino acids inside the Can f 1 and Fel d 7 calyx. Consistent with simulations, the stoichiometry of oleic acid-binding is 2:1 (fatty acid: protein) for Can f 1 and Fel d 7. Discussion: The results provide valuable insights into the determinants of selectivity and candidate ligands for pet lipocalin allergens Can f 1 and Fel d 7.
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