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首页> 外文期刊>Molecular Immunology >Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7.
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Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7.

机译:Asp159是尘螨过敏原Der f 7的IgE结合和交叉反应性表位的关键核心氨基酸。

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摘要

Der f 7 and Der p 7 are important house dust mite allergens with known structure and suggested biological function recently. However, their IgE-binding determinants remain unknown. The purpose of this study is to identify the IgE-reactive epitopes of Der f 7 and the determinants of IgE-mediated cross-reactivity between Der f 7 and Der p 7. IgE-reactive determinants were identified by immunodot blot inhibition using synthetic overlapping peptides, allergen mutants, and a Der f 7 structural model. Our results showed that synthetic peptides with sequence (156)SILDP(160) on Der f 7 bind IgE in two of the 30 asthmatic serum samples tested. Recombinant Der f 7 I157A, L158A, or D159A mutants have reduced IgE-binding activity. Inhibition experiments confirmed Asp159 as a critical core residue for IgE-binding. Among Der p 7, Der f 7 and Der f 7 mutants with single substitution between residues 156 and 160, only the D159A mutant cannot inhibit significantly IgE-binding against Der p 7. Therefore, Asp159 contributes to IgE-mediated cross-reactivity between Der f 7 and Der p 7. The structural model constructed for Der f 7 suggests that the IgE-binding epitope forms a loop-like structure on the surface of the molecule. In conclusion, Asp 159 is a critical core residue of an IgE-binding and IgE-mediated cross-reactive epitope (156)SILDP(160) of Der f 7. Results obtained from this study provide more information on molecular and structural features related to allergenicity, underlying basis of IgE cross-reactivity between allergens, and in designing safer immunotherapy.
机译:Der f 7和Der p 7是重要的屋尘螨过敏原,具有已知的结构和最近的生物学功能。但是,它们的IgE绑定决定因素仍然未知。本研究的目的是鉴定Der f 7的IgE反应性抗原决定簇以及Der f 7和Der p 7之间IgE介导的交叉反应性的决定因素。使用合成的重叠肽通过免疫斑点印迹法鉴定IgE反应性决定因素。 ,变应原突变体和Der f 7结构模型。我们的结果表明,Der f 7上具有序列(156)SILDP(160)的合成肽与30种哮喘血清样品中的2种结合IgE。重组Der f 7 I157A,L158A或D159A突变体的IgE结合活性降低。抑制实验证实Asp159是IgE结合的关键核心残基。在残基156和160之间具有单个取代基的Der p 7,Der f 7和Der f 7突变体中,只有D159A突变体不能显着抑制针对Der p 7的IgE结合。 f 7和Der p7。为Der f 7构建的结构模型表明,结合IgE的表位在分子表面形成环状结构。总之,Asp 159是Der f 7的IgE结合和IgE介导的交叉反应性表位(156)SILDP(160)的关键核心残基。从这项研究获得的结果提供了有关与以下物质有关的分子和结构特征的更多信息变应原性,变应原之间IgE交叉反应的基础以及设计更安全的免疫疗法。

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