Trans-Dominant Inhibitory Human Immunodeficiency Virus Type 1 Protease Monomers Prevent Protease Activation and Virion Maturation

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 22; pp. 10069 - 10073
• Main Authors: Babe, Lilia M., Rose, Jason, Craik, Charles S.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 24.10.1995; National Acad Sciences; National Academy of Sciences
• Subjects: AIDS/HIV; Animals; Asparagine; Aspartic Acid; Binding Sites; Biochemistry; Cell Line; Cell lines; Cercopithecus aethiops; COS cells; DNA; DNA, Viral - metabolism; Escherichia coli; Gene Expression; HeLa Cells; HIV; HIV 1; HIV Protease - biosynthesis; HIV Protease - metabolism; HIV-1 - enzymology; HIV-1 - physiology; Human immunodeficiency virus; human immunodeficiency virus 1; Humans; Kinetics; Macromolecular Substances; Monomers; Plasmids; Point Mutation; Polyproteins; Recombinant Proteins - biosynthesis; Recombinant Proteins - metabolism; RNA, Viral - biosynthesis; T lymphocytes; Transfection; Virion - physiology; Virions

Production of infectious human immunodeficiency virus (HIV) requires proper polyprotein processing by the dimeric viral protease. The trans-dominant inhibitory activity of a defective protease monomer with the active site Asp-25 changed to Asn was measured by transient transfection. A proviral plasm...