From the 1Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan; 2JST Innovation Plaza Hiroshima, Higashi-Hiroshima, Japan; 3Nishikawa Rubber Co. Ltd., Hiroshima, Japan; 4Takanobashi Central Hospital, Hiroshima, Japan.
World Allergy Organ J. 2010 Nov;3(11):262-5. doi: 10.1097/WOX.0b013e318201d81d.
Protease activities in allergen sources are thought to be involved in triggering allergic inflammation through the disruption of epithelial barrier or the induction of proinflammatory cytokines. Protease allergens may also work as type 2 helper T cell (TH2) adjuvants through the cleavage of cell surface receptors. Here, we report molecular cloning and immunochemical characterization of a new Japanese cedar (Cryptomeria japonica) pollen allergen (CPA9) homologous to serine protease, which is initially found as a high IgE-binding spot on our two-dimensional (2-D) IgE immunoblotting map. The cpa9 cDNA encoded a 757 amino acid polypeptide showing a significant sequence identity with plant subtilisin-like serine protease family members including melon major allergen Cuc m 1. We found that native CPA9 purified from C. japonica pollen showed a high IgE-binding frequency and IgE cross-reactivity with melon extract.
被认为参与通过破坏上皮屏障或诱导促炎细胞因子来触发过敏炎症的过敏原来源中的蛋白酶活性。蛋白酶过敏原也可能通过切割细胞表面受体作为 2 型辅助 T 细胞 (TH2) 佐剂发挥作用。在这里，我们报告了一种新的日本扁柏（Cryptomeria japonica）花粉过敏原（CPA9）的分子克隆和免疫化学特性，该过敏原与丝氨酸蛋白酶同源，最初在我们的二维（2-D）IgE 免疫印迹图谱上作为高 IgE 结合点发现。cpa9 cDNA 编码一个 757 个氨基酸的多肽，与包括甜瓜主要过敏原 Cuc m 1 在内的植物枯草杆菌样丝氨酸蛋白酶家族成员具有显著的序列同一性。我们发现从日本扁柏花粉中纯化的天然 CPA9 表现出与甜瓜提取物的高 IgE 结合频率和 IgE 交叉反应性。
