HUMAN IMMUNODEFICIENCY VIRUS PROTEASE EXPRESSED IN ESCHERICHIA-COLI EXHIBITS AUTOPROCESSING AND SPECIFIC MATURATION OF THE GAG PRECURSOR
HUMAN IMMUNODEFICIENCY VIRUS PROTEASE EXPRESSED IN ESCHERICHIA-COLI EXHIBITS AUTOPROCESSING AND SPECIFIC MATURATION OF THE GAG PRECURSOR
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DOI：
10.1073/pnas.84.24.8903
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发表时间：
1987-12-01
影响因子：
11.1
通讯作者：
ROSENBERG, M
中科院分区：
文献类型：
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作者：
DEBOUCK, C;GORNIAK, JG;ROSENBERG, M
人类免疫缺陷病毒(HIV)和所有逆转录病毒的成熟GAG和Pol蛋白都是由大的GAG和GAG-POL蛋白前体经翻译后切割而来的。这种必需的蛋白分解过程需要一种高度特异的、病毒编码的蛋白酶。在这项研究中，HIV蛋白水解酶基因产物在大肠杆菌中表达，并被证明可以从一个更大的前体自动催化其成熟。此外，这种细菌产生的HIV蛋白水解酶在大肠杆菌中共表达时，专门处理HIV P55 Gag多蛋白前体。该系统将允许对HIV蛋白酶进行详细的结构和功能分析，并为开发针对这种关键病毒酶的潜在治疗剂提供一种简单的分析方法。
The mature gag and pol proteins of human immunodeficiency virus (HIV) and all retroviruses derive from large gag and gag-pol polyprotein precursors by posttranslational cleavage. A highly specific, virally encoded protease is required for this essential proteolytic processing. In this study, the HIV protease gene product was expressed in Escherichia coli and shown to autocatalyze its maturation from a larger precursor. In addition, this bacterially produced HIV protease specifically processed an HIV p55 gag polyprotein precursor when coexpressed in E. coli. This system will allow detailed structure-function analysis of the HIV protease and provides a simple assay for the development of potential therapeutic agents directed against this critical viral enzyme.