Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1

Abstract

Background IgE-mediated allergy to fish is a frequent cause of lifethreatening allergic reactions. Allergen-specific immunotherapeutic approaches often make use of modified proteins that were designed to be hypoallergenic to reduce the risk of reactions. Since allergen-specific immunotherapy is the only treatment that provides long-term clinical benefits, determining the structure and molecular dynamics characteristics of allergens is necessary to understand how they interact with IgE and how to interfere with it by modifying the IgE-binding sites. b-parvalbumins represent one of the largest animal food-allergen families and are considered cross-reactive pan-allergens in fish. The b-parvalbumin structure is characterized by the presence of three EF-hand motifs (helix-loop-helix) called AB, CD and EF, but only CD and EF can chelate calcium ions. In order to contribute to the understanding of the allergenicity and the importance of the Ca2+-binding motifs for the stability of b-parvalbumins, we studied the major allergen of cod (Gadus morhua), Gad m 1, a member of the parvalbumin protein family