Abstract
Nonspecific lipid transfer proteins (nsLTPs) are basic proteins, stabilized by four disulfide bonds, and are expressed throughout the plant kingdom. These proteins are also known as important allergens in fruits and tree nuts. In this study, the nsLTP from hazelnuts, Cor a 8, was purified and its crystal structure determined. The protein is stable at low pH and refolds after thermal denaturation. Molecular dynamics simulations were used to provide an insight into conformational changes of Cor a 8 upon ligand binding. When known epitope areas from Pru p 3 were compared to those of Cor a 8, differences were obvious, which may contribute to limited cross-reactivity between peach and hazelnut allergens. Differences in epitope regions may contribute to limited cross-reactivity between Cor a 8 and nsLTPs from other plant sources. The structure of Cor a 8 represents the first resolved structure of a hazelnut allergen.
Highlights
As the number of people affected by food allergies increases worldwide, with its prevalence estimated to be between 1 and 8% of the world’s population,[1,2] hazelnut (Corylus avellana) continues to lead as one of the most common allergen sources.[3−6] Currently (June 2015), 10 allergens from C. avellana are registered with the Allergen Nomenclature Sub-Committee of the International Union of Immunological Societies (IUIS),[7] belonging to a variety of protein families
Hazelnut allergy has mainly been associated with crossreactive IgE to Bet v 1 and Bet v 2, usually causing mild symptoms known as oral allergy syndrome
In areas lacking exposure to birch pollen, hazelnut allergies are mostly associated with more severe reactions[13] and linked to sensitization to the nonspecific lipid transfer protein Cor a 8.14
Summary
As the number of people affected by food allergies increases worldwide, with its prevalence estimated to be between 1 and 8% of the world’s population,[1,2] hazelnut (Corylus avellana) continues to lead as one of the most common allergen sources.[3−6] Currently (June 2015), 10 allergens from C. avellana are registered with the Allergen Nomenclature Sub-Committee of the International Union of Immunological Societies (IUIS),[7] belonging to a variety of protein families Five of these allergens (Cor a 1,8 Cor a 8,9 Cor a 9,10 Cor a 11,11 and Cor a 1410,12) are considered to be the major culprits associated with reactions in patients sensitized to hazelnut. This structural feature facilitates resistance to thermal treatment and digestion, which could explain their involvement in more severe allergic reactions.[20,21]
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