Identification of Der f 23 as a new major allergen of Dermatophagoides farinae
Identification of Der f 23 as a new major allergen of Dermatophagoides farinae
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Der f 23 鉴定为粉尘螨新主要过敏原
DOI：
10.3892/mmr.2019.10305
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发表时间：
2019-08-01
影响因子：
3.4
通讯作者：
Ji，Kunmei
中科院分区：
文献类型：
--
作者：
He，Yongshen;Dou，Chuanran;Ji，Kunmei
屋尘螨（HDM）是世界范围内常见的过敏原来源。目前，在国际公认的37个HDM过敏原群中，有32个已在粉尘螨中鉴定出来。本研究描述了第一个已知的D。粉尘螨23型变应原（Der f 23）。克隆、表达并纯化重组Der f 23蛋白（rDer f 23）. rDer f 23的开放阅读框为525个碱基对，编码174个氨基酸的蛋白质（GenBank登录号，KU166910.1）。ELISA结果表明，72/129 HDM过敏血清样品（55.8%）具有特异性免疫球蛋白E（sIgE）结合活性的rDer f 23。此外，3/10例HDM过敏患者（30%）对rDer f 23表现出阳性皮肤点刺试验反应。IgE蛋白质印迹分析数据表明，仅4/11 HDM过敏血清具有阳性sIgE结合结果。序列同源性分析表明，Der f 23中多了一个Der f 23中没有的P2区（Ser 56-Thr 117）。pteronyssinus同系物，可能影响sIgE结合。Der f 23ΔP2表现出与HDM过敏性血清结合，而单独的P2肽不结合。Der f 23 ΔP2（P2区截短的Der f 23）的sIgE结合能力比Der f 23强。这些数据表明Der f 23中的P2区减弱IgE结合能力。总之，本研究的结果表明，Der f 23是主要的HDM过敏原，主要具有构象sIgE结合表位。Der f 23的过敏原鉴定及其被世界卫生组织/国际免疫学会联合会数据库收录有助于为HDM过敏性疾病的诊断和治疗提供理论基础。
House dust mites (HDM) are common allergen sources worldwide. At present, 32 of the 37 internationally recognized HDM allergen groups have been identified in Dermatophagoides farinae. The present study study describes the identification of the first known D. farinae Group 23 allergen (Der f 23). Recombinant Der f 23 protein (rDer f 23) was cloned, expressed and purified. The open reading frame of rDer f 23 was 525 base pairs and encoded a 174-amino acid protein (GenBank accession no., KU166910.1). ELISAs indicated that 72/129 HDM allergic serum samples (55.8%) had specific immunoglobulin E (sIgE) binding activity to rDer f 23. Additionally, 3/10 patients with HDM allergies (30%) exhibited positive skin prick test reactions to rDer f 23. IgE western blot analysis data suggested that only 4/11 HDM allergic sera had a positive sIgE binding result. Sequence homology analysis revealed an extra P2 region (Ser56-Thr117) in Der f 23 that was not present in the D. pteronyssinus homolog, which may affect sIgE binding. Der f 23ΔP2 demonstrated binding with HDM allergic sera, whereas the P2 peptide alone did not. The sIgE binding ability of Der f 23 ΔP2 (Der f 23 with a truncated P2 region) was more marked compared with that of Der f 23 in an IgE ELISA. These data indicate that P2 region in Der f 23 attenuates IgE binding ability. In conclusion, the results of the present study indicate that Der f 23 is a major HDM allergen with predominantly conformational sIgE binding epitopes. The allergenic identification of Der f 23 and its inclusion in World Health Organization/International Union of Immunological Societies database contributes to the theoretical basis underlying the diagnosis and treatment of HDM allergic diseases.