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首页> 外文期刊>Biological chemistry >A nonspecific, single-stranded nuclease activity with characteristics of a topoisomerase found in a major grass pollen allergen: possible biological significance.
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A nonspecific, single-stranded nuclease activity with characteristics of a topoisomerase found in a major grass pollen allergen: possible biological significance.

机译：一种主要草粉花粉过敏原中具有拓扑异构酶特征的非特异性单链核酸酶活性：可能的生物学意义。

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摘要

The major allergen from timothy grass pollen, Phlp5b (Phleum pratense), was shown to exhibit ribonuclease activity. It turned out that the C-terminal portion of this molecule was the biologically active domain. Here evidence is presented that the allergen is a single-stranded, sugar-nonspecific nuclease with topoisomerase activity. An isomerase-specific active site was identified, and a non-active mutant was constructed by site directed mutagenesis, and showed no nucleolytic activity. In contrast to the wild type (WT), the mutant did not dimerize. Although the binding capacity of IgE antibodies toward the mutant was reduced as compared to the WT, the allergenic activity was retained. We conclude that the allergen Phlp5b is a single-stranded nuclease with an unusual topoisomerase-like activity. This biological activity is not by itself connected to the allergenicity of the molecule. Whether the enzymatic activity is responsible for the induction of the allergic sensitization and inflammation remains an open question.
机译：豆科植物花粉的主要变应原Phlp5b（Phleum pratense）具有核糖核酸酶活性。事实证明，该分子的C端部分是生物活性结构域。此处提供的证据表明，过敏原是具有拓扑异构酶活性的单链糖非特异性核酸酶。鉴定了一个异构酶特异性活性位点，并且通过位点定向诱变构建了非活性突变体，并且没有显示出溶核活性。与野生型（WT）相反，该突变体不二聚。尽管与WT相比，IgE抗体对突变体的结合能力降低了，但变应原活性得以保留。我们得出的结论是，变应原Phlp5b是具有不寻常的拓扑异构酶样活性的单链核酸酶。这种生物活性本身并不与分子的致敏性有关。酶活性是否引起过敏性致敏和炎症仍然是一个悬而未决的问题。

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