Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro.
Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro.
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DOI：
10.1186/1471-2091-13-3
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发表时间：
2012-01-31
期刊：
影响因子：
--
通讯作者：
Mareš M
中科院分区：
文献类型：
--
作者：
Pytelková J;Lepšík M;Sanda M;Talacko P;Marešová L;Mareš M
污染储存食品的储存螨的酶过敏原的特征很差。我们描述了生化和免疫学特性的本地α-淀粉酶过敏原Aca的4粗粉螨，医学上重要的存储螨。A. siro产生高水平的α-淀粉酶活性，这归因于Aca s4。对该酶进行了纯化，并通过蛋白质测序和LC-MS/MS分析进行了鉴定。Aca s 4表现出独特的抑制模式和不寻常的α-淀粉分解活性，对氯离子激活的敏感性低。Aca s 4的同源建模揭示了氯离子结合位点的结构变化，这可能是导致这种激活模式的原因。Aca s 4被屋尘螨过敏患者的IgE识别，并发现了与屋尘螨4组过敏原交叉反应的潜在表位。由于其高产量和IgE反应性，Aca s 4可能与过敏性超敏反应相关。
Enzymatic allergens of storage mites that contaminate stored food products are poorly characterized. We describe biochemical and immunological properties of the native alpha-amylase allergen Aca s 4 from Acarus siro, a medically important storage mite. A. siro produced a high level of alpha-amylase activity attributed to Aca s 4. This enzyme was purified and identified by protein sequencing and LC-MS/MS analysis. Aca s 4 showed a distinct inhibition pattern and an unusual alpha-amylolytic activity with low sensitivity to activation by chloride ions. Homology modeling of Aca s 4 revealed a structural change in the chloride-binding site that may account for this activation pattern. Aca s 4 was recognized by IgE from house dust mite-sensitive patients, and potential epitopes for cross-reactivity with house dust mite group 4 allergens were found. We present the first protein-level characterization of a group 4 allergen from storage mites. Due to its high production and IgE reactivity, Aca s 4 is potentially relevant to allergic hypersensitivity.
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影响因子：
6.1
作者：
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通讯作者：
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影响因子：
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作者：
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通讯作者：
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