NDLI: Active human immunodeficiency virus protease is required for viral infectivity.

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Active human immunodeficiency virus protease is required for viral infectivity.

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Active human immunodeficiency virus protease is required for viral infectivity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Heimbach, J. C. Sigal, I. S. Scolnick, E. M. Dixon, R. A. Emini, E. A. Davis, L. J. Schleif, W. A. Kohl, N. E.
Description	Author Affiliation: Kohl NE ( Department of Molecular Biology, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.);
Abstract	Retroviral proteins are synthesized as polyprotein precursors that undergo proteolytic cleavages to yield the mature viral proteins. The role of the human immunodeficiency virus (HIV) protease in the viral replication cycle was examined by use of a site-directed mutation in the protease gene. The HIV protease gene product was expressed in Escherichia coli and observed to cleave HIV gag p55 to gag p24 and gag p17 in vitro. Substitution of aspartic acid residue 25 (Asp-25) of this protein with an asparagine residue did not affect the expression of the protein, but it eliminated detectable in vitro proteolytic activity against HIV gag p55. A mutant HIV provirus was constructed that contained the Asn-25 mutation within the protease gene. SW480 human colon carcinoma cells transfected with the Asn-25 mutant proviral DNA produced virions that contained gag p55 but not gag p24, whereas virions from cells transfected with the wild-type DNA contained both gag p55 and gag p24. The mutant virions were not able to infect MT-4 lymphoid cells. In contrast, these cells were highly sensitive to infection by the wild-type virions. These results demonstrate that the HIV protease is an essential viral enzyme and, consequently, an attractive target for anti-HIV drugs.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	85
Language	English
Publisher	National Academy of Sciences
Publisher Date	1988-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endopeptidases Physiology HIV Enzymology Viral Proteins Asparagine Binding Sites Genetics Metabolism Gene Products, Gag HIV Protease Protein Precursors Proviruses Recombinant Fusion Proteins Retroviridae Proteins Virulence Virus Replication Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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