Structural highlights
Function
MAL11_MALDO
Publication Abstract from PubMed
More than 70% of birch pollen-allergic patients develop allergic cross-reactions to the major allergen found in apple fruits (Malus domestica), the 17.5 kDa protein Mal d 1. Allergic reactions against this protein result from initial sensitization to the major allergen from birch pollen, Bet v 1. Immunologic cross-reactivity of Bet v 1-specific IgE antibodies with Mal d 1 after apple consumption can subsequently provoke severe oral allergic syndromes. This study presents the three-dimensional NMR solution structure of Mal d 1 (isoform Mal d 1.0101, initially cloned from 'Granny Smith' apples). This protein is composed of a seven-stranded antiparallel beta-sheet and three alpha-helices that form a large internal cavity, similar to Bet v 1 and other cross-reactive food allergens. The Mal d 1 structure provides the basis for elucidating the details of allergic cross-reactivity between birch pollen and apple allergens on a molecular level.
Structure of the Major Apple Allergen Mal d 1.,Ahammer L, Grutsch S, Kamenik AS, Liedl KR, Tollinger M J Agric Food Chem. 2017 Mar 1;65(8):1606-1612. doi: 10.1021/acs.jafc.6b05752., Epub 2017 Feb 15. PMID:28161953[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahammer L, Grutsch S, Kamenik AS, Liedl KR, Tollinger M. Structure of the Major Apple Allergen Mal d 1. J Agric Food Chem. 2017 Mar 1;65(8):1606-1612. doi: 10.1021/acs.jafc.6b05752., Epub 2017 Feb 15. PMID:28161953 doi:http://dx.doi.org/10.1021/acs.jafc.6b05752