Synthetic Approaches to the Biological Activity of β-Lactoglobulin in Human Allergy to Cows' Milk

Abstract

WORK carried out in this laboratory since 1962 on the structure of the active sites in the allergens involved in the hypersensitivity syndrome of atopy in man (asthma, hay fever, atopic dermatitis group) has been based on the observation that the physicochemical properties of these allergens differ significantly from those of other (glyco)-protein antigens¹. Specifically, the early postulate of N-glycosidic structural centres formed by Maillard reactions between ɛ-amino groups of lysine residues and reducing sugar has recently been substantiated by studying the absorption characteristics in the ultra-violet of purified inhalant and food allergens in relation to those of synthetic model compounds^2,3. Because isolation studies on the atopic allergen in cows' milk had shown the skin-reactive allergen to reside largely in the β-lactoglobulin fraction⁴, an attempt was made to increase its specific activity by synthetically incorporating N-glycosidically bound carbohydrates into the molecule.