2MC9

Cat r 1

2MC9 の概要

• エントリーDOI: 10.2210/pdb2mc9/pdb
• NMR情報: BMRB: 19432
• 分子名称: Peptidyl-prolyl cis-trans isomerase (1 entity in total)
• 機能のキーワード: cyclophilin, allergen, isomerase
• 由来する生物種: Catharanthus roseus (chatas,chula,old-maid,rosy periwinkle)
• 細胞内の位置: Cytoplasm: Q39613
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18844.28

構造登録者

Mueller, G.,London, R.,Ghosh, D. (登録日: 2013-08-16, 公開日: 2014-06-25, 最終更新日: 2024-05-15)

主引用文献

Ghosh, D.,Mueller, G.A.,Schramm, G.,Edwards, L.L.,Petersen, A.,London, R.E.,Haas, H.,Gupta Bhattacharya, S.
Primary identification, biochemical characterization, and immunologic properties of the allergenic pollen cyclophilin cat R 1.
J.Biol.Chem., 289:21374-21385, 2014

PubMed Abstract: Cyclophilin (Cyp) allergens are considered pan-allergens due to frequently reported cross-reactivity. In addition to well studied fungal Cyps, a number of plant Cyps were identified as allergens (e.g. Bet v 7 from birch pollen, Cat r 1 from periwinkle pollen). However, there are conflicting data regarding their antigenic/allergenic cross-reactivity, with no plant Cyp allergen structures available for comparison. Because amino acid residues are fairly conserved between plant and fungal Cyps, it is particularly interesting to check whether they can cross-react. Cat r 1 was identified by immunoblotting using allergic patients' sera followed by N-terminal sequencing. Cat r 1 (∼ 91% sequence identity to Bet v 7) was cloned from a cDNA library and expressed in Escherichia coli. Recombinant Cat r 1 was utilized to confirm peptidyl-prolyl cis-trans-isomerase (PPIase) activity by a PPIase assay and the allergenic property by an IgE-specific immunoblotting and rat basophil leukemia cell (RBL-SX38) mediator release assay. Inhibition-ELISA showed cross-reactive binding of serum IgE from Cat r 1-allergic individuals to fungal allergenic Cyps Asp f 11 and Mala s 6. The molecular structure of Cat r 1 was determined by NMR spectroscopy. The antigenic surface was examined in relation to its plant, animal, and fungal homologues. The structure revealed a typical cyclophilin fold consisting of a compact β-barrel made up of seven anti-parallel β-strands along with two surrounding α-helices. This is the first structure of an allergenic plant Cyp revealing high conservation of the antigenic surface particularly near the PPIase active site, which supports the pronounced cross-reactivity among Cyps from various sources.

PubMed: 24939849
DOI: 10.1074/jbc.M114.559971

実験手法

SOLUTION NMR