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首页> 外文期刊>Journal of Molecular Biology >The Disulphide Mapping, Folding and Characterisation of Recombinant Ber e 1, an Allergenic Protein, and SFA8, Two Sulphur-rich 2S Plant Albumins.
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The Disulphide Mapping, Folding and Characterisation of Recombinant Ber e 1, an Allergenic Protein, and SFA8, Two Sulphur-rich 2S Plant Albumins.

机译：重组Bere 1（一种过敏原蛋白）和SFA8（两个富含硫的2S植物白蛋白）的二硫化物定位，折叠和表征。

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摘要

We have cloned and expressed genes encoding the allergenic brazil nut 2S albumin (Ber e 1) and the sunflower albumin 8 (SFA8) in the methylotrophic yeast Pichia pastoris. We show that both proteins were secreted at high levels and that the purified proteins were properly folded. We also showed that Ber e 1 is glycosylated during secretion and that the glycan does not interfere with the folding or immunoreactivity. The disulphide map of the Ber e 1 protein was experimentally established and is in agreement with the conserved disulphide structure of other members of the 2S albumin family. A model three-dimensional structure of the allergen was generated. During the expression studies and through mutation we have also shown that alteration of the sequences around the Kex2 endoproteolytic processing site in the expressed fusion protein can compromise the secretion by targeting part of the protein for possible degradation. The secreted production of these properly folded sulphur-rich plant albumins presents an opportunity to delineate the attributes that make an allergen and to facilitate the diagnosis and therapy of type I allergy.
机译：我们已经在甲基营养型酵母巴斯德毕赤酵母中克隆并表达了编码变应性巴西坚果2S白蛋白（Ber e 1）和向日葵白蛋白8（SFA8）的基因。我们显示这两种蛋白质被高水平分泌，并且纯化的蛋白质被正确折叠。我们还表明，Ber e 1在分泌过程中被糖基化，并且聚糖不干扰折叠或免疫反应性。通过实验建立了Ber e 1蛋白的二硫化物图谱，并与2S白蛋白家族其他成员的保守二硫化物结构相符。产生了过敏原的模型三维结构。在表达研究和通过突变的过程中，我们还表明，表达的融合蛋白中Kex2内蛋白水解加工位点周围序列的改变可通过将蛋白的一部分靶向可能的降解而损害分泌。这些适当折叠的富含硫的植物白蛋白的秘密生产提供了一个机会，勾勒出构成过敏原的属性，并有助于I型过敏的诊断和治疗。

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