[根据热带地区感兴趣的过敏原设计的重组多表位蛋白的 Ige 反应性--初步发现]。

Luis Fang, Dalgys Martínez, Catherine Meza-Torres, Nicole Pereira-Sanandrés, Ana Moreno-Woo, Gloria Garavito, Eduardo Egea
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引用次数: 0

摘要

研究目的本研究的目的是设计一种来自淋蛔虫和 APD 过敏原的多表位蛋白,并初步评估其 IgE 反应性:利用计算工具,在 "硅 "中设计了一种分子,该分子含有来自于龙蝽和APD过敏原的多个 "T "表位,并利用大肠杆菌系统表达了这种多表位蛋白(MP1),然后使用Ni-NTA琼脂糖通过亲和层析进行纯化。通过点印迹法和间接酶联免疫吸附法,对来自哥伦比亚巴兰基亚的 HDM 过敏患者和非过敏者的血清中的抗 MP1 和抗 HDM 提取物 IgE 反应性进行了评估。过敏者对吸入过敏原(EUROLINE - Ref: DP 3704-1601-1 E)和螨虫特异性 IgE 的标准化皮肤测试呈阳性:结果:多表位(MP1)蛋白得到了高纯度表达和纯化。点印迹(Dot-Blot)结果显示,与 HDM 提取物相比,所有过敏患者的血清对 MP1 的 IgE 反应性都较低。通过酶联免疫吸附试验(ELISA),在对 HDM 过敏的患者血清中观察到的抗 MP1 IgE 浓度(中位数:270.86 ng/ml;IQR:90.3)明显低于抗 HDM IgE 水平(中位数:988.5 ng/ml;IQR:1117.6):结论:设计、表达和纯化了一种由蛔虫和HDM过敏原的多个表位组成的蛋白质。初步的点印迹(Dot-Blot)结果表明,与螨虫提取物相比,这种分子具有低过敏性和极低的 IgE 反应性。要更好地了解该分子诱导的免疫反应,还需要进一步的功能研究。
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[Ige reactivity of a recombinant multi-epitope protein designed from allergens of interest in the tropics - preliminary findings].

Objective: The objective of the present study was to design a multi-epitope protein from A. lumbricoides and APD allergens and to evaluate its IgE reactivity preliminarily.

Methods: Using computational tools, a molecule containing multiple "T" epitopes of allergens derived from A. lumbricoides and APD was designed "in silico" This multi-epitope protein (MP1) was expressed using an E. coli system and purified by affinity chromatography using Ni-NTA agarose. Anti-MP1 and anti-HDM extract IgE reactivity was evaluated by Dot-Blot and indirect ELISA from sera of HDM-allergic patients and non-allergic individuals from Barranquilla-Colombia. Allergic individuals had a positive skin test to a standardized battery of inhaled allergens (EUROLINE - Ref: DP 3704-1601-1 E) and mite- specific IgE.

Results: Multi-epitope (MP1) protein was expressed and purified with high purity. Dot-Blot result showed that all sera from allergic patients showed lower IgE reactivity to MP1 compared to HDM extract. By ELISA, significantly lower concentrations of anti-MP1 IgE (Median: 270.86 ng/ml; IQR: 90.3) were observed in contrast to anti-HDM IgE levels (Median: 988.5 ng/ml; IQR: 1117.6) in sera of patients allergic to HDM.

Conclusions: A protein composed of multiple epitopes of A. lumbricoides and HDM allergens was designed, expressed, and purified. Preliminary Dot-Blot results suggest that this molecule shows hypoallergenic properties with very low IgE reactivity compared to mite extract. Further functional studies are needed to understand better the immune response induced by this molecule.

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