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. 1989 Feb 11;17(3):969–978. doi: 10.1093/nar/17.3.969

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

D N SenGupta 1, R H Silverman 1
PMCID: PMC331716  PMID: 2922280

Abstract

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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Selected References

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