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Allergens and their associated small molecule ligands : their dual role in sensitization

Title data

Chruszcz, Maksymilian ; Chew, Fook Tim ; Hoffmann-Sommergruber, Karin ; Hurlburt, Barry K. ; Mueller, Geoffrey A. ; Pomés, Anna ; Rouvinen, Juha ; Villalba, Mayte ; Wöhrl, Birgitta M. ; Breiteneder, Heimo:
Allergens and their associated small molecule ligands : their dual role in sensitization.
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA; Department of Biological Sciences, National University of Singapore, Singapore; Division of Medical Biotechnology, Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria; Agricultural Research Service, Southern Regional Research Center, US Department of Agriculture, New Orleans, LA, USA; National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA; Indoor Biotechnologies, Inc., Charlottesville, VA, USA; Department of Chemistry, University of Eastern Finland, Joensuu, Finland; Department of Biochemistry and Molecular Biology, Universidad Complutense de Madrid, Madrid, Spain; Biochemie IV ‐ Biopolymere, Universität Bayreuth, Bayreuth, Germany; Division of Medical Biotechnology, Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria
In: Allergy European Journal Of Allergy And Clinical Immunology. (April 2021) .
ISSN 0105-4538
DOI: https://doi.org/10.1111/all.14861

Abstract in another language

Many allergens feature hydrophobic cavities that allow the binding of primarily hydrophobic small‐molecule ligands. Ligand‐binding specificities can be strict or promiscuous. Serum albumins from mammals and birds can assume multiple conformations that facilitate the binding of a broad spectrum of compounds. Pollen and plant food allergens of the family 10 of pathogenesis‐related proteins bind a variety of small molecules such as glycosylated flavonoid derivatives, flavonoids, cytokinins, and steroids in vitro. However, their natural ligand binding was reported to be highly specific. Insect and mammalian lipocalins transport odorants, pheromones, catecholamines, and fatty acids with a similar level of specificity, while the food allergen β‐lactoglobulin from cow's milk is notably more promiscuous. Non‐specific lipid transfer proteins from pollen and plant foods bind a wide variety of lipids, from phospholipids to fatty acids, as well as sterols and prostaglandin B2, aided by the high plasticity and flexibility displayed by their lipid‐binding cavities. Ligands increase the stability of allergens to thermal and proteolyticdegradation. They can also act as immunomodulatory agents that favor a Th2 polarization. In summary, ligand‐binding allergens expose the immune system to a variety of biologically active compounds whose impact on the sensitization process has not been well studied thus far.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Chair Biopolymers - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 04 May 2021 07:54
Last Modified: 04 May 2021 07:54
URI: https://eref.uni-bayreuth.de/id/eprint/65059