5FEG

Crystal structure of the dimeric allergen profilin (Hev b 8)

5FEG の概要

• エントリーDOI: 10.2210/pdb5feg/pdb
• 関連するPDBエントリー: 5FDS 5FEF
• 分子名称: Profilin-2 (1 entity in total)
• 機能のキーワード: actin binding protein, allergen, allergy, cross-reactivity, hev b 8
• 由来する生物種: Hevea brasiliensis (Para rubber tree)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28324.08

構造登録者

Mares-Mejia, I.,Rodriguez-Romero, A. (登録日: 2015-12-17, 公開日: 2016-09-14, 最終更新日: 2024-11-13)

主引用文献

Mares-Mejia, I.,Martinez-Caballero, S.,Garay-Canales, C.,Cano-Sanchez, P.,Torres-Larios, A.,Lara-Gonzalez, S.,Ortega, E.,Rodriguez-Romero, A.
Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms.
Sci Rep, 6:32552-32552, 2016

PubMed Abstract: Oligomerization of allergens plays an important role in IgE-mediated reactions, as effective crosslinking of IgE- FcεRI complexes on the cell membrane is dependent on the number of exposed B-cell epitopes in a single allergen molecule or on the occurrence of identical epitopes in a symmetrical arrangement. Few studies have attempted to experimentally demonstrate the connection between allergen dimerization and the ability to trigger allergic reactions. Here we studied plant allergenic profilins rHev b 8 (rubber tree) and rZea m 12 (maize) because they represent an important example of cross-reactivity in the latex-pollen-food syndrome. Both allergens in their monomeric and dimeric states were isolated and characterized by exclusion chromatography and mass spectrometry and were used in immunological in vitro experiments. Their crystal structures were solved, and for Hev b 8 a disulfide-linked homodimer was found. Comparing the structures we established that the longest loop is relevant for recognition by IgE antibodies, whereas the conserved regions are important for cross-reactivity. We produced a novel monoclonal murine IgE (mAb 2F5), specific for rHev b 8, which was useful to provide evidence that profilin dimerization considerably increases the IgE-mediated degranulation in rat basophilic leukemia cells.

PubMed: 27586352
DOI: 10.1038/srep32552

実験手法

X-RAY DIFFRACTION (2.802 Å)