NMR resonance assignments of the major apple allergen Mal d 1

详细信息    查看全文

• 作者：Linda Ahammer ; Sarina Grutsch ; Martin Tollinger
• 关键词：NMR resonance assignment ; Mal d 1 ; Apple ; Allergen
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：10
• 期：2
• 页码：287-290
• 全文大小：603 KB
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X
• 卷排序：10

文摘

The major apple allergen Mal d 1 is the predominant cause of apple (Malus domestica) allergies in large parts of Europe and Northern America. Allergic reactions against this 17.5 kDa protein are the consequence of initial sensitization to the structurally homologous major allergen from birch pollen, Bet v 1. Consumption of apples can subsequently provoke immunologic cross-reactivity of Bet v 1-specific antibodies with Mal d 1 and trigger severe oral allergic syndroms, affecting more than 70 % of all individuals that are sensitized to birch pollen. While the accumulated immunological data suggest that Mal d 1 has a three-dimensional fold that is similar to Bet v 1, experimental structural data for this protein are not available to date. In a first step towards structural characterization of Mal d 1, backbone and side chain 1H, 13C and 15N chemical shifts of the isoform Mal d 1.0101 were assigned. The NMR-chemical shift data show that this protein is composed of seven β-strands and three α-helices, which is in accordance with the reported secondary structure of the major birch pollen allergen, indicating that Mal d 1 and Bet v 1 indeed have similar three-dimensional folds. The next stage in the characterization of Mal d 1 will be to utilize these resonance assignments in solving the solution structure of this protein.