Crystal structure and some properties of a major house dust mite allergen, Derf 2.
Crystal structure and some properties of a major house dust mite allergen, Derf 2.
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DOI：
10.1016/j.bbrc.2005.11.065
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发表时间：
2006-01
影响因子：
3.1
通讯作者：
Masashi Suzuki;Yoshimasa Tanaka;S. Korematsu;B. Mikami;N. Minato
中科院分区：
文献类型：
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作者：
Masashi Suzuki;Yoshimasa Tanaka;S. Korematsu;B. Mikami;N. Minato
Pyroglyphid屋尘螨是屋尘中过敏原的主要来源。螨过敏原致敏并诱发大部分过敏性疾病患者的哮喘、鼻炎和湿疹。在这里，一个主要的螨过敏原，Derf 2，来自粉尘螨的晶体结构，解决了单一同晶置换法与异常散射（SIRAS）在2.1纳米分辨率。本研究还表明，过敏原的构象是至关重要的，在确定的Th 1/Th 2漂移的基础上的理化和免疫学分析。这表明，刚性折叠和单一分散的结构是过敏原产生Th 2型细胞所必需的，而构象变体蛋白导致Th 1偏斜，而不管相同的氨基酸序列如何。这种结构/功能关系可能使我们能够开发一种新的策略，用于对屋尘螨过敏原引发的过敏性疾病患者进行脱敏治疗。
Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1Å resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens.