Journal
JOURNAL OF VIROLOGY
Volume 74, Issue 1, Pages 541-546Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.74.1.541-546.2000
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Funding
- NIAID NIH HHS [R01 AI036636, AI01339, AI36636, R01 AI040317, AI40317] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI036636, R01AI040317] Funding Source: NIH RePORTER
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Retroviral RNA encapsidation depends on the specific binding of Gag proteins to packaging (Jr) signals in genomic RNA. We investigated whether an in vitro-selected, high-affinity RNA ligand for the nucleocapsid (NC) portion of the Gag protein from human immunodeficiency virus type 1 (HIV-1) could mediate packaging into HIV-1 virions. We find that this ligand can functionally substitute for one of the Gag-binding elements (termed SL3) in the HIV-1 phi locus to support packaging and viral infectivity in cis. By contrast, this ligand, which fails to dimerize spontaneously in vitro, is unable to replace a different phi element (termed SL1) which is required for both Gag binding and dimerization of the HIV-1 genome. A single point mutation within the ligand that eliminates high-affinity in vitro Gag binding also abolishes its packaging activity at the SL3 position. These results demonstrate that specific binding of Gag or NC protein is a critical determinant of genomic RNA packaging.
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