RT Journal Article
T1 Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1-like protein family.
A1 Stemeseder, Teresa
A1 Freier, Regina
A1 Wildner, Sabrina
A1 Fuchs, Julian E
A1 Briza, Peter
A1 Lang, Roland
A1 Batanero, Eva
A1 Lidholm, Jonas
A1 Liedl, Klaus R
A1 Campo, Paloma
A1 Hawranek, Thomas
A1 Villalba, Mayte
A1 Brandstetter, Hans
A1 Ferreira, Fatima
A1 Gadermaier, Gabriele
K1 Molecular Conformation
K1 Plant Proteins
K1 Structure-Activity Relationship
AB Knowledge of structural and immunological features of allergens is important for understanding IgE sensitization and disease-eliciting mechanisms of allergenic molecules. Despite the fact that Ole e 1–like proteins are driving type I allergies within several pollen sources [1,2], there is currently no information regarding their tertiary structure. Ole e 1–like proteins are characterized by three conserved disulfide bonds and the [EQT]-G-X-V-Y-C-D-[TNP]-C-R consensus pattern, while their biological function remains unknown. To date, 14 allergenic members of this protein family, all originating from pollen, have been reported (www.allergen.org). These proteins exhibit varying degrees of sequence identity, typically high among Oleaceae species (>82%) but medium/low between botanically distant plants (25% to 60%).
PB Elsevier
YR 2016
FD 2016-12-10
LK http://hdl.handle.net/10668/10675
UL http://hdl.handle.net/10668/10675
LA en
NO Stemeseder T, Freier R, Wildner S, Fuchs JE, Briza P, Lang R, et al. Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1-like protein family. J Allergy Clin Immunol. 2017 Jul;140(1):277-280
DS RISalud
RD Apr 7, 2025