Moloney murine leukemia virus protease expressed in bacteria is enzymatically active

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

Research output: Contribution to journalArticle

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

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Peptide Hydrolases
Bacteria
pol Gene Products
Virion
gag Gene Products
Moloney murine leukemia virus
Virus Activation
Polyproteins
Proteins
Cell Membrane
Moloney murine leukemia virus protease
Escherichia coli

ASJC Scopus subject areas

  • Genetics
  • Applied Microbiology and Biotechnology

Cite this

Moloney murine leukemia virus protease expressed in bacteria is enzymatically active. / Cannon, K.; Qin, L.; Schumann, G.; Boeke, J. D.

In: Archives of Virology, Vol. 143, No. 2, 1998, p. 381-388.

Research output: Contribution to journalArticle

Cannon, K. ; Qin, L. ; Schumann, G. ; Boeke, J. D. / Moloney murine leukemia virus protease expressed in bacteria is enzymatically active. In: Archives of Virology. 1998 ; Vol. 143, No. 2. pp. 381-388.
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