Moloney murine leukemia virus protease expressed in bacteria is enzymatically active

被引：5

作者：

Cannon, K ^{[1
]}

Qin, L ^{[1
]}

Schumann, G ^{[1
]}

Boeke, JD ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Baltimore, MD 21205 USA

来源：

ARCHIVES OF VIROLOGY | 1998年 / 143卷 / 02期

关键词：

D O I：

10.1007/s007050050294

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Replication of Moloney murine leukemia virus requires a readthrough translation mechanism to generate the Gag-Pol polyprotein. One of the final products of this polyprotein is the protease (PR), which is required to generate the mature virion proteins. The assembly of Gag and Gag-Pol polyproteins into a virion followed by activation of the viral protease is necessary to produce a mature, infectious particle. These events are believed to occur near the cell membrane just prior to the budding of the virion. We report here the autoproteolytic activity of the viral PR when a Gag-PR fusion protein is expressed in E. coli. Efficient cleavage at the p12/CA, CA/NC and NC/PR junctions was observed. Thus the Moloney murine leukemia virus PR is capable of cleaving its substrates in the absence of specific host factors.

引用

页码：381 / 388

页数：8

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