Nucleic Acids Research, 1989, Vol. 17, No. 3 969-978
© 1989
ENZYMOLOGY |
Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA
Department of Pathology, Uniformed Services University of the Health Sciences 4301 Jones Bridge Road, Bethesda, MD 20814-4799, USA
*To whom correspondence should be addressed
Received November 7, 1988. Revised January 3, 1989. Accepted January 3, 1989.
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.
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