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

1 Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary 2 HIV Drug Resistant Program, National Cancer Institute at Frederick, MD, USA 3 Department of Biology, Georgia State University, Atlanta, GA,...

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Published in:Journal of general virology 2006-05, Vol.87 (5), p.1321-1330
Main Authors: Feher, Anita, Boross, Peter, Sperka, Tamas, Miklossy, Gabriella, Kadas, Janos, Bagossi, Peter, Oroszlan, Stephen, Weber, Irene T, Tozser, Jozsef
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biological and medical sciences
Carbamates - pharmacology
Escherichia coli
Escherichia coli - metabolism
Fundamental and applied biological sciences. Psychology
Gene Products, gag - genetics
Gene Products, gag - metabolism
HIV Protease - metabolism
HIV Protease Inhibitors - pharmacology
Human immunodeficiency virus 1
Human viral diseases
Humans
Hydrogen-Ion Concentration
Infectious diseases
Leukemia Virus, Murine - enzymology
Leukemia Virus, Murine - immunology
Medical sciences
Mice
Microbiology
Miscellaneous
Molecular Sequence Data
Murine leukemia virus
NIH 3T3 Cells
Oligopeptides - metabolism
Peptide Hydrolases - biosynthesis
Peptide Hydrolases - genetics
Peptide Hydrolases - metabolism
Recombinant Proteins - biosynthesis
Recombinant Proteins - metabolism
Species Specificity
Sulfonamides - pharmacology
Viral diseases
Viral diseases of the lymphoid tissue and the blood. Aids
Virology
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Summary:1 Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary 2 HIV Drug Resistant Program, National Cancer Institute at Frederick, MD, USA 3 Department of Biology, Georgia State University, Atlanta, GA, USA Correspondence József Tözsér tozser{at}indi.biochem.dote.hu 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.
ISSN:0022-1317
1465-2099
DOI:10.1099/vir.0.81382-0