INSITU PROCESSING OF A RETROVIRAL NUCLEOCAPSID PROTEIN BY THE VIRAL PROTEINASE

被引：39

作者：

ROBERTS, MM

COPELAND, TD

OROSZLAN, S

机构：

[1] Laboratory of Molecular Virology and Carcinogenesis, NCI-Fredenck Cancer Research and Development Center, Frederick, MD

来源：

PROTEIN ENGINEERING | 1991年 / 4卷 / 06期

关键词：

RETROVIRAL CAPSID; RETROVIRAL NUCLEOCAPSID PROTEIN; RETROVIRAL PROTEINASE;

D O I：

10.1093/protein/4.6.695

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The proteolytic processing pathway of the nucleocapsid protein (NC) by the viral proteinase within intact capsids of equine infectious anemia virus (EIAV) is presented. The cleavage sites are located at the carboxyl side of the first cysteine residue within the zinc-finger domains. EIAV is used as a model to predict similar NC cleavages in other retroviruses, including human immunodeficiency virus (HIV). The observed cleavages suggest a previously unrecognized function of the retroviral proteinase that may be crucial for replication during the early stages of the virus life-cycle (i.e. reverse transcription/integration).

引用

页码：695 / 700

页数：6

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