ArticleScientific reports2019
Crystal structure of the dog allergen Can f 6 and structure-based implications of its cross-reactivity with the cat allergen Fel d 4.
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, 25 citations in OpenAlex.
- Human Allergy to Cats and Dogs: Molecular and Environmental Determinants, Diagnosis, and Precision Management.Veterinary sciences · 2026Review
- Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.Allergy · 2026Article
- Advance in Managing Indoor Cat Allergen Proteins: Molecular Insights, Detection, and Control.International journal of molecular sciences · 2025Review
- Recombinant Hypoallergenic Cat Allergy Vaccines.Allergy · 2025Article
- Fel d 1 specific IgE measurement for dog exclusive owners co-sensitized to dog and cat.The World Allergy Organization journal · 2024Article
- Do commercial dog extracts cross-react withAllergy and asthma proceedings · 2024Article
- Allergies to Allergens from Cats and Dogs: A Review and Update on Sources, Pathogenesis, and Strategies.International journal of molecular sciences · 2024Review
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- The Acari Hypothesis, V: deciphering allergenicity.Frontiers in allergy · 2024Article
- Allergenic Activity of Individual Cat Allergen Molecules.International journal of molecular sciences · 2023Article
- Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7.Frontiers in allergy · 2023Article
- Animal Allergens, Endotoxin, and β-(1,3)-Glucan in Small Animal Practices: Exposure Levels at Work and in Homes of Veterinary Staff.Annals of work exposures and health · 2022Article
- Human allergy to cats: A review for veterinarians on prevalence, causes, symptoms and control.Journal of feline medicine and surgery · 2022Review
- Molecular diagnosis in cat allergy.World journal of methodology · 2021Review
- The Molecular Allergen Recognition Profile in China as Basis for Allergen-Specific Immunotherapy.Frontiers in immunology · 2021Review
- The role of allergen-specific IgE in predicting allergic symptoms on dog and cat exposure among Korean pet exhibition participants.The World Allergy Organization journal · 2020Article
- Review
- The allergenic activity and clinical impact of individual IgE-antibody binding molecules from indoor allergen sources.The World Allergy Organization journal · 2020Review
- Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6.PloS one · 2019Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several dog allergens cause allergic reactions in humans worldwide. Seven distinct dog allergens, designated Canis familiaris allergen 1 to 7 (Can f 1-Can f 7), have been identified thus far. Can f 6 shows high sequence similarity and cross-reactivity with Fel d 4 and Equ c 1, major cat and horse allergens, respectively. This study was conducted on the allergenic epitopes of Can f 6 based on its structural characterization. We demonstrated that sera from 18 out of 38 (47%) dog-sensitized patients reacted to recombinant Can f 6 protein (rCan f 6). We then determined the crystal structure of rCan f 6 by X-ray crystallography, which exhibited a conserved tertiary structural architecture found in lipocalin family proteins. Based on the tertiary structure and sequence similarities with Fel d 4 and Equ c 1, we predicted three IgE-recognizing sites that are possibly involved in cross-reactivity. Substituting three successive amino acids in these sites to triple alanine decreased IgE reactivity to the allergen. However, the degree of reduction in IgE reactivity largely depended on the site mutated and the serum used, suggesting that Can f 6 is a polyvalent allergen containing multiple epitopes and Can f 6-reactive sera contain varied amounts of IgE recognising individual Can f 6 epitopes including those predicted in this study. We also demonstrated that the predicted epitopes are partly involved in IgE cross-reactivity to Fel d 4. Interestingly, the effect of the mutation depended on whether the protein was structured or denatured, indicating that the bona fide tertiary structure of Can f 6 is essential in determining its IgE epitopes.
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