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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
Cyclophilins, a new family of cross-reactive allergens
Sabine Flückiger1, Helmi Fijten, Paul Whitley
1Swiss Institute of Allergy and Asthma Research (SIAF), Davos, Switzerland.
Abstract:
Type I allergic reactions occur by immediate release of anaphylactogenic mediators due to cross-linking of IgE bound to the high-affinity Fc(epsilon)RI on the surface of effector cells of sensitized individuals after allergen exposure. IgE-mediated hypersensitivity against normally innocuous environmental antigens is of clinical importance because of an increasing incidence of asthma and severe atopic diseases causing raising health care burdens to the society. A vast variety of different molecular structures has been shown to be able to induce hypersensitivity reactions. However, the high structural homology between phylogenetically conserved allergenic proteins present in different, apparently unrelated sources of exposure seems to play an important role in IgE-mediated poly-sensitization. These allergen families, formally termed pan-allergens, represent proteins sharing a high degree of sequence homology. Here we report cloning, production and serological investigations of a new pan-allergen family, the cyclophilins, found to be cross-reactive across species including humans. IgE-mediated cross-reactivity against autoantigens may contribute to perpetuation of severe atopic disorders even in the absence of exogenous allergen exposure. The molecular definition of pan-allergen families may substantially contribute to reduce the number of structures needed for diagnosis and therapy of allergic diseases based on highly pure, standardized recombinant allergens.
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