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Allergy

Title:		Allergens and their associated small molecule ligands-their dual role in sensitization
Author(s):		Chruszcz M; Chew FT; Hoffmann-Sommergruber K; Hurlburt BK; Mueller GA; Pomes A; Rouvinen J; Villalba M; Wohrl BM; Breiteneder H;
Address:		"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, Universitat Bayreuth, Bayreuth, Germany"
Journal Title:		Allergy
Year:		2021
Volume:		20210502
Issue:		8
Page Number:		2367 - 2382
DOI:		10.1111/all.14861
ISSN/ISBN:		1398-9995 (Electronic) 0105-4538 (Print) 0105-4538 (Linking)
Abstract:		"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 beta-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/or proteolytic degradation. 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"
Keywords:		*Allergens/metabolism Animals Cattle Female *Food Hypersensitivity Ligands Pollen Protein Binding Pr-10 group 2 house dust mite allergens lipocalin nsLTP serum albumin;
Notes:		"MedlineChruszcz, Maksymilian Chew, Fook Tim Hoffmann-Sommergruber, Karin Hurlburt, Barry K Mueller, Geoffrey A Pomes, Anna Rouvinen, Juha Villalba, Mayte Wohrl, Birgitta M Breiteneder, Heimo eng R01 AI077653/AI/NIAID NIH HHS/ Z99 ES999999/ImNIH/Intramural NIH HHS/ ZIA ES102906/ImNIH/Intramural NIH HHS/ Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Review Denmark 2021/04/19 Allergy. 2021 Aug; 76(8):2367-2382. doi: 10.1111/all.14861. Epub 2021 May 2"