Structural Characterization of the Tetrameric form of the Major Cat Allergen Fel d 1

Kaiser, Liselotte; Veličković, Tanja Ćirković; Badia-Martinez, Daniel; Adédoyin, Justus; Thunberg, Sarah; Hallén, Dan; Berndt, Kurt D.; Grönlund, Hans; Gafvelin, Guro; Hage, Marianne van; Achour, Adnane

doi:10.1016/j.jmb.2007.04.074

Cited by 60 publications

(85 citation statements)

References 60 publications

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“…clusters together with LPS to form larger complexes that then promotes greater clustering of TLR4-bearing lipid rafts, leading to increased receptor activation [25]. Fel d 1 belongs to the secretoglobin family of proteins with a putative lipid-binding pocket, where lipid components may interact [26,27]. Notably, there are many other allergens that belong to protein families with lipid-binding properties such as lipocalins, apolipophorin, secretoglobins, 2S albumins, non-specific lipidbinding proteins (nsLTPs) and Bet v 1-like proteins.…”

Section: Toll-like Receptorsmentioning

confidence: 99%

“…Notably, there are many other allergens that belong to protein families with lipid-binding properties such as lipocalins, apolipophorin, secretoglobins, 2S albumins, non-specific lipidbinding proteins (nsLTPs) and Bet v 1-like proteins. For instance, Can f 6 (dog), belonging to the protein family of lipocalin [27], has similar TLR4-stimulatory properties as Fel d 1, but also shows some MD-2-independent effects [25]. Lipid-binding properties were attributed to allergenic 2S albumins and nsLTPs (e.g.…”

Section: Toll-like Receptorsmentioning

confidence: 99%

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What makes an allergen?

Scheurer

Toda

Vieths

2015

Clin Experimental Allergy

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SummaryAllergic diseases are an immune disorder reacting to certain type of allergen(s). Remarkably only a small number of proteins of the plant and animal proteome act as allergens. Therefore, allergens have been clustered according to their common structural, biochemical and functional features. Evidence has accumulated that some allergens possess intrinsic adjuvant properties to stimulate the innate immunity. The adjuvant properties appear to contribute to the allergenicity of the respective proteins, namely the ability to cause allergic sensitization in susceptible subjects or allergic reactions in sensitized individuals. Here, we discuss how allergens interact with the innate immune cells, in particular dendritic cells and epithelial cells, via binding to pattern recognition receptors, exhibiting proteolytic activities and/or inducting type 2 innate lymphoid cells (ILC2), thereby contributing to the sensitization and development of allergic diseases.

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Section: Toll-like Receptorsmentioning

confidence: 99%

Section: Toll-like Receptorsmentioning

confidence: 99%

What makes an allergen?

Scheurer

Toda

Vieths

2015

Clin Experimental Allergy

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“…Oligomerization is a common phenomenon among allergens and has often been observed in the X-ray crystal structures of allergens or in solution [58,59,60]. Since oligomerization in X-ray crystal structures does not always reflect the oligomeric state in physiological conditions, techniques such as size exclusion chromatography or light scattering can be used to assess oligomerization of allergens in solution.…”

Section: Relevance Of Oligomerization For Allergic Diseasementioning

confidence: 99%

Relevant B Cell Epitopes in Allergic Disease

Pomés¹

2009

Int Arch Allergy Immunol

135

106

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The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the use of overlapping synthetic peptides, recombinant allergenic fragments or unfolded allergens. These approaches led to the identification of mostly linear epitopes and are useful for food allergens that undergo digestion or food processing. For inhaled allergens, conformational epitopes appear to be the primary targets of IgE responses. Knowledge of the molecular structure of allergens alone and in complex with antibodies that interfere with IgE antibody binding is important to understand the immune recognition of B cell-antigenic determinants on allergens and the design of recombinant allergens for immunotherapy. Starting with the molecular cloning and expression of allergens, and with the advent of X-ray crystallography and nuclear magnetic resonance techniques, we have been able to visualize conformational epitopes on allergens.

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“…Over the years, Fel d 1 has been extensively characterized, both by biochemical and immunological methods such as CD spectrum [30] and amino acid sequencing [31], cloning [32], chrystallography [33,34,35], analysis of T-cell epitope repertoires [36,37], serological measurements of patients’ IgE antibodies [17,38], as well as epitope mapping by monoclonal antibodies [39,40,41]. …”

Section: Biochemical Characterization Of Fel Dmentioning

confidence: 99%

“…Fel d 1 and orthologues of the uteroglobin protein family, such as rabbit uteroglobin, the human Clara cell protein, CC16, and the mouse androgen-binding protein all include a cavity, which may harbour small ligands [43,46,47,48]. Recently, the quaternary structure of Fel d 1 was reported, highlighting 2 new structural aspects [34]. First, it was shown that the close molecular interaction by the dimer formation causes a profound alteration of the 2 pockets, creating a smaller 350- and a larger 750-Å 3 compartment.…”

Section: Biochemical Characterization Of Fel Dmentioning

confidence: 99%

The Major Cat Allergen, Fel d 1, in Diagnosis and Therapy

Grönlund

Saarne

Gafvelin

et al. 2009

Int Arch Allergy Immunol

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Sensitization to cat is a common cause of allergic disease all over the world. Symptoms range from mild rhinoconjunctivitis to potentially life-threatening asthmatic exacerbations. In vivo and in vitro diagnostics of cat allergy is currently based on cat dander extract. As allergen extracts from natural sources are heterogeneous in composition, the allergen content may vary. With the introduction of allergens produced by recombinant techniques, a large panel of recombinant allergenic molecules including the major cat allergen, recombinant Fel d 1, has become available for immunological investigations, diagnosis and treatment. Studies have shown that this single allergen, which belongs to the uteroglobin protein family, is at least as good as cat dander extract in identifying cat-allergic patients. The introduction of recombinant Fel d 1-based tests into clinical practice will increase our knowledge of this single allergen molecule as a diagnostic tool and improve the selection for therapy of cat allergy. Several different modes for allergen-specific immunotherapy of cat allergy based on Fel d 1 have been developed. These include Fel d 1 hypoallergens and allergen constructs where Fel d 1 is coupled to immunomodulatory proteins or carriers. The approaches have been evaluated in experimental in vitro and in vivo model systems with promising results. In addition, immunotherapy with Fel d 1 peptides containing T-cell epitopes has been tested in clinical trials. After initial problems with adverse reactions, more recent data show that peptide immunotherapy modulates the immune response to Fel d 1 and reduces early- and late-phase effector reactions in cat-allergic patients.

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Structural Characterization of the Tetrameric form of the Major Cat Allergen Fel d 1

Cited by 60 publications

References 60 publications

What makes an allergen?

What makes an allergen?

Relevant B Cell Epitopes in Allergic Disease

The Major Cat Allergen, Fel d 1, in Diagnosis and Therapy

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