Abstract
Fagales allergens belonging to the Bet v 1 family account responsible for the majority of spring pollinosis in the temperate climate zones in the Northern hemisphere. Among them, Fag s 1 from beech pollen is an important trigger of Fagales pollen associated allergic reactions. The protein shares high similarity with birch pollen Bet v 1, the best-characterized member of this allergen family. Of note, recent work on Bet v 1 and its homologues found in Fagales pollen demonstrated that not all allergenic members of this family have the capacity to induce allergic sensitization. Fag s 1 was shown to bind pre-existing IgE antibodies most likely primarily directed against other members of this multi-allergen family. Therefore, it is especially interesting to compare the structures of Bet v 1-like pollen allergens, which have the potential to induce allergic sensitization with allergens that are mainly cross-reactive. This in the end will help to identify allergy eliciting molecular pattern on Bet v 1-like allergens. In this work, we report the 1H, 15N and 13C NMR assignment of beech pollen Fag s 1 as well as the secondary structure information based on backbone chemical shifts.
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Acknowledgments
Christian Doppler Research Association, Austria; Biomay AG, Vienna, Austria; Austrian Science Fund (FWF). CNPq, FAPERJ, and INBEB, Brazil.
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Moraes, A.H., Asam, C., Batista, A. et al. 1H, 13C and 15N resonance assignments and second structure information of Fag s 1: Fagales allergen from Fagus sylvatica . Biomol NMR Assign 10, 45–48 (2016). https://doi.org/10.1007/s12104-015-9634-y
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DOI: https://doi.org/10.1007/s12104-015-9634-y