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