Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease

Anita Fehér, Péter Boross, Tamás Sperka, Gabriella Miklóssy, János Kádas, Péter Bagossi, Stephen Oroszlan, Irene T. Weber, József Tözsér

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The protease (PR) of Murine leukemia virus (MLV) was expressed in Escherichia coli, purified to homogeneity and characterized by using various assay methods, including HPLC-based, photometric and fluorometric activity measurements. The specificity of the bacterially expressed PR was similar to that of virion-extracted PR. Compared with human immunodeficiency virus type 1 (HIV-1) PR, the pH optimum of the MLV enzyme was higher. The specificity of the MLV PR was further compared with that of HIV-1 PR by using various oligopeptides representing naturally occurring cleavage sites in MLV and HIV-1, as well as by using bacterially expressed proteins having part of the MLV Gag. Inhibitors designed against HIV-1 PR were also active on MLV PR, although all of the tested ones were substantially less potent on this enzyme than on HIV-1 PR. Nevertheless, amprenavir, the most potent inhibitor against MLV PR, was also able to block Gag processing in MLV-infected cells. These results indicate that, in spite of the similar function in the life cycle of virus infection, the two PRs are only distantly related in their specificity.

Original languageEnglish
Pages (from-to)1321-1330
Number of pages10
JournalJournal of General Virology
Volume87
Issue number5
DOIs
Publication statusPublished - May 1 2006

ASJC Scopus subject areas

  • Virology

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