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 1H, 13C and 15N resonances of this protein and predicted its secondary structure. The NMR-chemical shift data indicate that Bet v 1.0102 is composed of three α-helices and a seven stranded β-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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Ahammer L,Grutsch S,Wallner M,Ferreira F,Tollinger Mdoi
10.1007/s12104-017-9754-7subject
Has Abstractpub_date
2017-10-01 00:00:00pages
231-234issue
2eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-017-9754-7journal_volume
11pub_type
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