Related ArticlesNMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1.
Biomol NMR Assign. 2017 Aug 14;:
Authors: Ahammer L, Grutsch S, Wallner M, Ferreira F, Tollinger M
Abstract
In Northern America and Europe a great number of people are suffering from birch pollen allergy and pollen related food allergies. The trigger for these immunological reactions is the 17.5*kDa major birch pollen allergen Bet v 1, which belongs to the family of PR-10 (pathogenesis-related) proteins. In nature, Bet v 1 occurs as a mixture of various isoforms that possess different immunological properties despite their high sequence identities. Bet v 1.0102 (Bet v 1d), which is investigated here, is a hypoallergenic isoform of Bet v 1 and a potential candidate for allergen-specific immunotherapy. We assigned the backbone and side chain (1)H, (13)C and (15)N resonances of this protein and predicted its secondary structure. The NMR-chemical shift data indicate that Bet v 1.0102 is composed of three ?-helices and a seven stranded ?-sheet, in agreement with the known structure of the hyperallergenic isoform Bet v 1.0101 (Bet v 1a). Our resonance assignments create the foundation for detailed characterization of the dynamic properties of Bet v 1 isoforms by NMR relaxation measurements.
PMID: 28808910 [PubMed - as supplied by publisher]
[NMR paper] NMR resonance assignments of the major apple allergen Mal d 1.
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Biomol NMR Assign. 2016 May 11;
Authors: Ahammer L, Grutsch S, Tollinger M
Abstract
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...
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[NMR paper] X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy.
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Nat Struct Biol. 1996 Dec;3(12):1040-5
Authors: Gajhede M, Osmark P, Poulsen FM, Ipsen H, Larsen JN, Joost van Neerven RJ, Schou C, Løwenstein H, Spangfort MD
The three-dimensional structure of the major birch pollen allergen, the 17,500 M(r) acidic protein Bet v 1 (from the birch, Betula verrucosa), is presented as determined both in the crystalline state by X-ray diffraction and in...
NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1.
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