title: Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: Anita
authors.initials: A
authors.lastname: Fehér
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: Péter
authors.initials: P
authors.lastname: Boross
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: Tamás
authors.initials: T
authors.lastname: Sperka
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: Gabriella
authors.initials: G
authors.lastname: Miklóssy
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: János
authors.initials: J
authors.lastname: Kádas
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: Péter
authors.initials: P
authors.lastname: Bagossi
authors.affiliation: HIV Drug Resistant Program, National Cancer Institute at Frederick, MD, USA.
authors.forename: Stephen
authors.initials: S
authors.lastname: Oroszlan
authors.affiliation: Department of Biology, Georgia State University, Atlanta, GA, USA.
authors.forename: Irene T
authors.initials: IT
authors.lastname: Weber
authors.affiliation: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.
authors.forename: József
authors.initials: J
authors.lastname: Tözsér
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002219:Carbamates / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism; D005663:Furans; D015683:Gene Products, gag / Q000235:genetics / Q000378:metabolism; D016333:HIV Protease / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009052:Leukemia Virus, Murine / Q000201:enzymology* / Q000276:immunology; D051379:Mice; D008969:Molecular Sequence Data; D041681:NIH 3T3 Cells; D009842:Oligopeptides / Q000378:metabolism; D010447:Peptide Hydrolases / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D013045:Species Specificity; D013449:Sulfonamides / Q000494:pharmacology
chemical_list: D002219:Carbamates; D005663:Furans; D015683:Gene Products, gag; D017320:HIV Protease Inhibitors; D009842:Oligopeptides; D011994:Recombinant Proteins; D013449:Sulfonamides; C095108:amprenavir; D010447:Peptide Hydrolases; D016333:HIV Protease