Occupational Asthma Reference

Chruszcz M, Chew FT, Hoffmann-Sommergruber K, Hurlburt BK, Mueller GA, Pomés A, Rouvinen J, Villalba M, Wöhrl BM, Breiteneder H, Allergens and their associated small molecule ligands - their dual role in sensitization, Allergy, 2021;:,10.1111/all.14861
(Plain text: Chruszcz M, Chew FT, Hoffmann-Sommergruber K, Hurlburt BK, Mueller GA, Pomes A, Rouvinen J, Villalba M, Wohrl BM, Breiteneder H, Allergens and their associated small molecule ligands - their dual role in sensitization, Allergy)

Keywords: review, flavinoids, cytokinins, odorants, pheromones, non-specific lipid transfer, review

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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 ß-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.

Plain text: 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 b-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.

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