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首页> 外文期刊>Protein Expression and Purification >Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli
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Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli

机译：与麦芽糖结合蛋白融合的功能活跃的恶性疟原虫恶性疟原虫2在大肠杆菌中的可溶性表达

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摘要

Falcipain-2 (fp2) is a hemoglobinase required for supplying peptides and amino acids for the proliferation of Plasmodium falciparum in blood. The prospect of circumventing its activity thereby serves as a potential strategy for mining drugs for anti-malarial therapy. However, to date, efforts to express soluble and active fp2 in Escherichia coli have been futile. To overcome this problem, fp2 was expressed under an array of conditions including the exploitation of multiple gene constructs in eukaryotic and prokaryotic hosts. A series of experiments led to the finding that the placement of maltose-binding protein (MBP) before the fp2 mature domain was best in availing the soluble expression of the protease. The results also indicate that the prodomain impaired the bacterial expression of the protease and the amino acid residues at the N-terminal segment of mature fp2 can have a significant effect on the folding and solubility of the enzyme. The overexpressed MBP-fp2 fusion protein was purified and shown to be functionally active, providing a very useful alternative to the use of resolubilized enzyme for future study of structure and function of fp2. (C) 2003 Elsevier Inc. All rights reserved. [References: 26]
机译：Falcipain-2（fp2）是一种血红蛋白酶，为血液中恶性疟原虫的增殖提供肽和氨基酸所需。因此，规避其活性的前景成为挖掘抗疟疾药物的潜在策略。然而，迄今为止，在大肠杆菌中表达可溶性和活性fp2的努力是徒劳的。为了克服这个问题，在一系列条件下表达了fp2，包括在真核和原核宿主中利用多个基因构建体。一系列实验导致发现，在fp2成熟结构域之前放置麦芽糖结合蛋白（MBP）最佳利用了蛋白酶的可溶性表达。结果还表明，该前结构域损害了蛋白酶的细菌表达，并且成熟fp2的N-末端区段上的氨基酸残基可以对酶的折叠和溶解性具有显着影响。纯化了过表达的MBP-fp2融合蛋白，显示其具有功能活性，为将来进一步研究fp2的结构和功能提供了一种非常有用的替代方法，可替代溶解化酶的使用。 （C）2003 Elsevier Inc.保留所有权利。 [参考：26]

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