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Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA.




 

Nucleic Acids Res. 1989 Feb 11;17(3):969-78. Unique Identifier :

Human immunodeficiency virus-1 (HIV-1) leader RNA, which contains double-stranded regions due to inverted repeats, was shown to activate the dsRNA-dependent enzymes associated with the interferon system. HIV-1 leader RNA produced in vitro using SP6 RNA polymerase was characterized using probes for antisense and sense-strand RNA. The RNA preparation was free from significant levels of antisense RNA. HIV-1 leader RNA was shown to activate dsRNA-dependent protein kinase in a cell-free system from interferon-treated HeLa cells. Affinity resins, consisting of HIV-1 leader RNA covalently attached to cellulose, immobilized and activated dsRNA-dependent protein kinase and 2-5A-synthetase. HIV-1 leader RNA, therefore, may be a contributing factor in the mechanism by which interferon inhibits HIV replication.

Cell-Free System Enzyme Activation Enzymes, Immobilized Hela Cells Human HIV-1/*GENETICS Interferon Type I/*PHYSIOLOGY Plasmids Protein Kinases/METABOLISM Resins, Synthetic RNA, Double-Stranded/*PHYSIOLOGY RNA, Messenger/BIOSYNTHESIS/*PHYSIOLOGY Support, U.S. Gov't, Non-P.H.S. Support, U.S. Gov't, P.H.S. 2',5'-Oligoadenylate Synthetase JOURNAL ARTICLE



 




Information in this article was accurate in June 30, 1989. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.