Journal
VIRUSES-BASEL
Volume 13, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/v13122389
Keywords
HIV-1; packaging; in-gel SHAPE; Gag; NC; RNA structure; dimerisation
Categories
Funding
- Eric Reid Fund for Methodology grant from the Biochemical Society UK
- UK Medical Research Council [MR/N022939/1]
- NIHR Cambridge BRC [RCAG/18]
- National Research Foundation Singapore
- Singapore Ministry of Education, under their Research Centres of Excellence initiative
- Clinical Academic Reserve
- MRC [MR/N022939/1] Funding Source: UKRI
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HIV-1 packages two copies of its gRNA into virions through an interaction with the Gag protein, essential for virion infectivity. A lack of structural techniques previously hindered the understanding of the stepwise packaging process. The study using in-gel SHAPE technique sheds light on the initiation of HIV-1 packaging and the interaction between RNA and Gag protein.
HIV-1 packages two copies of its gRNA into virions via an interaction with the viral structural protein Gag. Both copies and their native RNA structure are essential for virion infectivity. The precise stepwise nature of the packaging process has not been resolved. This is largely due to a prior lack of structural techniques that follow RNA structural changes within an RNA-protein complex. Here, we apply the in-gel SHAPE (selective 2'OH acylation analysed by primer extension) technique to study the initiation of HIV-1 packaging, examining the interaction between the packaging signal RNA and the Gag polyprotein, and compare it with that of the NC domain of Gag alone. Our results imply interactions between Gag and monomeric packaging signal RNA in switching the RNA conformation into a dimerisation-competent structure, and show that the Gag-dimer complex then continues to stabilise. These data provide a novel insight into how HIV-1 regulates the translation and packaging of its genome.
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