Abstract
In large parts of Europe, Northern America and China people are suffering from allergies after consuming certain kinds of fruits and vegetables. Typical allergic symptoms range from scratching and itching of the throat to severe symptoms like rhino conjunctivitis and anaphylaxis. For hazelnuts (Corylus avellana), these allergies result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent development of allergic cross-reactions to proteins that are similar in their three-dimensional structure to the sensitizing protein Bet v 1. The cross-reactive proteins in hazelnut are the four isoforms Cor a 1.04 with a molecular weight of about 17.5 kDa. Significant differences regarding the immunologic behavior of these proteins have been reported. In this work we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of these four isoforms, Cor a 1.0401, Cor a 1.0402, Cor a 1.0403, and Cor a 1.0404 by solution NMR spectroscopy. The chemical shift data confirm the characteristic Bet v onefold for all four isoforms, consisting of seven β-strands that are separated by two short α-helices, along with a long C-terminal α-helix. These data provide the basis for a comparative structural and dynamic analysis of these proteins by NMR in order to characterize their different immunologic cross-reactivities on a molecular level.
Highlights
In the northern hemisphere, pollinosis caused by sensitization to birch pollen is the most common allergy
In 62–98% of birch pollen allergic patients IgE-specific antibodies are directed at the protein Bet v 1, the major birch pollen allergen (Ipsen and Lowenstein 1983; Moverare et al 2002)
Immunological cross-reactivity of Bet v 1 specific antibodies (IgE) to proteins that are present in fruits and nuts can provoke additional allergic reactions in patients suffering from birch pollinosis
Summary
Pollinosis caused by sensitization to birch pollen is the most common allergy. Immunological cross-reactivity of Bet v 1 specific antibodies (IgE) to proteins that are present in fruits and nuts can provoke additional allergic reactions in patients suffering from birch pollinosis. These foods typically trigger oral allergic syndromes (OAS), including itching and scratching of the oral cavity, directly after consumption (Mari et al 2005). Allergic cross-reactivities are associated with the class 10 of pathogenesis related (PR) proteins in hazelnut and hazel pollen (Vieths et al 2002), whose expression is induced by environmental or pathogenic stress. In this work we present the solution NMR backbone and side-chain assignments of the four recombinantly expressed isoforms of Cor a 1.04
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