NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04

• DOI: 10.1007/s12104-019-09918-6
• Publication Date: 2019-11-05T20:02:41Z
• Authors: Sebastian Führer; Ricarda Zeindl; Martin Tollinger
• Keywords: 0303 health sciences; 03 medical and health sciences; Corylus; Proton Magnetic Resonance Spectroscopy; Protein Isoforms; Allergens; Nuclear Magnetic Resonance, Biomolecular; Article; Protein Structure, Secondary; Plant Proteins

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.