Recombinant expression of HIV-1 protease using soluble fusion tags in Escherichia coli: A vital tool for functional characterization of HIV-1 protease

被引：3

作者：

Eche, Simeon ^{[1
]}

Gordon, Michelle L. ^{[1
]}

机构：

[1] Univ KwaZulu Natal, Sch Lab Med & Med Sci, ZA-4001 Durban, South Africa

来源：

VIRUS RESEARCH | 2021年 / 295卷

关键词：

HIV-1; protease; Escherichia coli; Soluble fusion tags; GLUTATHIONE-S-TRANSFERASE; INCLUSION-BODY FORMATION; VIRUS TYPE-1 PROTEASE; HIGH-LEVEL EXPRESSION; X-RAY; BIOLOGICAL EVALUATION; MAMMALIAN PROTEINS; CHEMICAL-SYNTHESIS; PEPTIDE-SYNTHESIS; PURIFICATION;

D O I：

10.1016/j.virusres.2020.198289

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

HIV-1 protease expression in the laboratory is demanding because of its high cytotoxicity, making it difficult to express in bacterial expression systems such as Escherichia coli. To overcome these challenges, HIV-1 protease fusion with solubility enhancing tags helps to mitigate its cytotoxic effect and drive its expression as a soluble protein. Therefore, this review focuses on the expression of bioactive HIV-1 protease using solubility-enhancing fusion tags in Escherichia coli and summarises the characteristic features of the different common fusion tags that have been used in the expression of HIV-1 protease. This review will assist researchers with their choice of protein fusion tag for HIV-1 protease expression.

引用

页数：9

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