免疫球蛋白E 皮质映射和结构-过敏性关系分析过敏原 Scy p 9 p 9
Xin-Rong He1, Yang Yang1,2, Ye-Xin Chen1
1College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Jimei University, Xiamen, Fujian 361021, China.
Journal of agricultural and food chemistry
|November 6, 2023
概括
研究了filamin C (Scy p 9) 的过敏性. 关键氨基酸突变减少了IgE结合,并确定了特定的线性表位,澄清了结构-过敏性关系.
科学领域:
- 免疫学 免疫学 免疫学
- 生物化学 生物化学
- 分子生物学分子生物学
背景情况:
- 来自*Scylla paramamosain* (Scy p 9) 的胺C是一种已知的过敏原.
- 之前的研究在一个主要的过敏原区域中发现了六个线性IgE表位.
- 然而,Scy p 9的IgE表位和结构与过敏性关系的确切性仍然不清楚.
研究的目的:
- 为了阐明IgE表位和Filamin C的结构-过敏性关系 (Scy p9).
- 为了确定关键的氨基酸和参与IgE结合和过敏作用的区域.
主要方法:
- 关键氨基酸在预测的构造性表观体内进行局部导向的突变发生.
- 评估野生类型和突变蛋白质的IgE结合能力和表面水性.
- 使用合成的线性表位的验证.
- 将IgE表位图映射到Scy的三级结构上 p 9.
主要成果:
- 鉴定出疏水性键对于维持蛋白质构成至关重要.
- 突变E216A,T270A,Y699A和V704A显著降低了IgE结合能力和表面水性.
- 确认了10个线性表位,其中L-AA187-205表现出最强的IgE结合.
- IgE表位位于三级结构的突出的表面上,表明IgE结合的可访问性.
- 鉴定到的表位体在不同的丝基因中显示出很高的保护性.
结论:
- 这项研究澄清了Scy p 9的IgE表位和结构-过敏性关系.
- 特定的氨基酸残留物和线性表位对Scy p 9过敏性至关重要.
- 这些发现为了解胺C的过敏性和开发诊断或治疗策略提供了基础.
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