尘螨过敏原Der p 2线性表位肽及其硝基化产物与IgE结合能力
The IgE binding capability of the linear epitope peptides and their nitration products of house dust mite allergy Der p 2
李志琪 1杨方星1
作者信息
- 1. 浙江大学环境与资源学院环境健康研究所,污染环境修复与生态健康教育部重点实验室,杭州,310058
- 折叠
摘要
许多过敏原可以介导I型超敏反应,通过与IgE特异性结合,引起过敏症状.过敏原与细胞表面的特异性IgE结合的部分叫做表位,其与IgE的结合能力可以表征过敏原致敏性的强弱.Derp2是一种重要的屋尘螨过敏原,其线性表位中含有的酪氨酸可被空气中的NO2和O3硝基化,从而影响线性表位与IgE的结合能力.本实验研究了 Derp 2的线性表位及其硝基化产物与IgE的结合能力.研究发现,Derp2的两条表位多肽可以有效地结合IgE,硝基化表位多肽的IgE结合能力显著高于未硝基化的表位多肽,且不同位点的硝基化对于IgE结合能力的增强程度也不同.结果表明,硝基化能够位点特异性地增强Derp2的致敏性.
Abstract
Many allergies can cause type Ⅰ hypersensitivity,through binding to specific-IgE and leading the allergic symptoms.The binding ability of epitope,which is the portion of an allergen protein that binds with specific IgE on cell surface,to IgE can indicate the allergenicity of allergen.Der p 2 is an important house dust mite allergic protein.The tyrosine residues in the epitopes of Der p 2 can be nitrated by airborne NO2 and O3,which could subsequently promote the allergenicity.In this study,the abilities of the epitopes and their nitrated products to bind to the specific IgE were investigated.The results reveal that the two epitope peptides effectively bound to the specific IgE,and the IgE binding capacities of the nitrated epitope peptides were significantly higher than the non-nitrated forms.Besides,the contribution of nitration to the enhancement of IgE binding capacity depended on the location of tyrosine.These findings suggest that nitration can enhance the allergenicity of Der p 2 in a tyrosine site-specific manner.
关键词
Derp2/线性表位/硝基化/位点特异性/IgE/致敏性Key words
Der p 2/linear epitope/nitration/site-specific/IgE/allergenicity引用本文复制引用
基金项目
浙江省自然科学基金公益项目(LGF21B070007)
出版年
2024
NETL
NSTL
万方数据