Abstract
Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens.
Highlights
The major birch pollen allergen Bet v 1 is a member of the ubiquitous family of pathogenesis-related plant proteins of class-10 (PR-10) [1]
PR-10 proteins are known to be involved in defense mechanisms of plants in response to various pathogens, low temperature, oxidative stress, or UV radiation [2,3,4]
We employed pulsed-field-gradient (PFG) translational diffusion NMR methods to probe the hydrodynamic radius of Bet v 1.0101 without and with ligand bound
Summary
The major birch pollen allergen Bet v 1 is a member of the ubiquitous family of pathogenesis-related plant proteins of class-10 (PR-10) [1]. PR-10 proteins consist of ~160 amino acids that fold into a highly conserved seven-stranded, highly curved, antiparallel b-sheet (b1–b7) along with two consecutive short a-helices (a1 and a2) and a long C-terminal helix (a3; Fig. 1) [1]. Together, these structural elements form an extended internal cavity that is capable of binding a variety of physiologically relevant amphipathic ligand molecules [1,5,6,7,8]. The 3D structures have been reported for various iso-
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