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Crystal structure of the dog allergen Can f 6 and structure-based implications of its cross-reactivity with the cat allergen Fel d 4
Open accessAbstract
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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Fel d 4 shows high sequence similarity to Can f 6 from dogs.
“Fel d 4 shows high sequence similarity to Can f 6 from dogs (Table 2) [58].”
From Advance in Managing Indoor Cat Allergen Proteins: Molecular Insights, Detection, and Control (2025) · cites this paper as [58]
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Metadata
- Authors
- Yamamoto, K., Ishibashi, O., Sugiura, K., Ubatani, M., Sakaguchi, M., Nakatsuji, M., Shimamoto, S., Noda, M., Uchiyama, S., Fukutomi, Y., Nishimura, S., & Inui, T.
- Affiliations
- Osaka Prefecture University (JP)
- Kindai University (JP)
- The University of Osaka (JP)
- National Sagamihara Hospital (JP)
- Corresponding author
- Inui, Takashi
- ORCID
- Venue
- Scientific Reports
- Published
- 2019-02-06
- Volume
- 9
- Issue
- 1
- Pages
- 1503-1503
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC6365566
- OpenAlex
- W2913646254
- Cited by
- 27
- References
- 32
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 5 · 2023: 3 · 2021: 6 · 2020: 6 · 2019: 1
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- MEXT | Japan Society for the Promotion of Science (16K08145, 24791017, 17K19329, 25242046)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Asthma and respiratory diseases
- Keywords
- dog allergen, cross-reactivity, IgE epitopes, crystal structure, recombinant allergens, IgE binding sites, canine allergy
- MeSH terms
- Allergens, Amino Acid Sequence, Animals, Epitopes, Cats, Cross Reactions, Dogs, Humans, Hypersensitivity, Immunoglobulin E, Models, Molecular, Species Specificity, Sequence Homology, Amino Acid, Crystallography, X-Ray, Lipocalins
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