Moloney murine leukemia virus protease expressed in bacteria is enzymatically active

K. Cannon, L. Qin, G. Schumann, J. D. Boeke

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Replication of Moloney murine leukemia virus requires a read-through 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.

    Original languageEnglish (US)
    Pages (from-to)381-388
    Number of pages8
    JournalArchives of Virology
    Volume143
    Issue number2
    DOIs
    StatePublished - 1998

    ASJC Scopus subject areas

    • Virology

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