scholarly journals Coordination of Genomic RNA Packaging with Viral Assembly in HIV-1

Viruses ◽  
2016 ◽  
Vol 8 (7) ◽  
pp. 192 ◽  
Author(s):  
Chris Hellmund ◽  
Andrew Lever
Keyword(s):  
Viral Assembly ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Hiv 1

scholarly journals New Structure Sheds Light on Selective HIV-1 Genomic RNA Packaging

Viruses ◽  
2015 ◽  
Vol 7 (8) ◽  
pp. 4826-4835 ◽  
Author(s):  
Erik Olson ◽  
William Cantara ◽  
Karin Musier-Forsyth
Keyword(s):  
Genomic Rna ◽  
Rna Packaging ◽  
Hiv 1

scholarly journals Distinct binding interactions of HIV-1 Gag to Psi and non-Psi RNAs: Implications for viral genomic RNA packaging

RNA ◽  
2013 ◽  
Vol 19 (8) ◽  
pp. 1078-1088 ◽  
Author(s):  
J. A. Webb ◽  
C. P. Jones ◽  
L. J. Parent ◽  
I. Rouzina ◽  
K. Musier-Forsyth
Keyword(s):  
Genomic Rna ◽  
Rna Packaging ◽  
Binding Interactions ◽  
Viral Genomic Rna ◽  
Hiv 1

scholarly journals Fullerene Derivatives Prevent Packaging of Viral Genomic RNA into HIV-1 Particles by Binding Nucleocapsid Protein

Viruses ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 2451
Author(s):  
Ivana Křížová ◽  
Alžběta Dostálková ◽  
Edison Castro ◽  
Jan Prchal ◽  
Romana Hadravová ◽  
...  
Keyword(s):  
Reverse Transcription ◽  
Biological Activities ◽  
Reverse Transcriptase Activity ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Fullerene Derivatives ◽  
Viral Genomic Rna ◽  
Anti Hiv ◽  
Hiv 1

Fullerene derivatives with hydrophilic substituents have been shown to exhibit a range of biological activities, including antiviral ones. For a long time, the anti-HIV activity of fullerene derivatives was believed to be due to their binding into the hydrophobic pocket of HIV-1 protease, thereby blocking its activity. Recent work, however, brought new evidence of a novel, protease-independent mechanism of fullerene derivatives’ action. We studied in more detail the mechanism of the anti-HIV-1 activity of N,N-dimethyl[70]fulleropyrrolidinium iodide fullerene derivatives. By using a combination of in vitro and cell-based approaches, we showed that these C70 derivatives inhibited neither HIV-1 protease nor HIV-1 maturation. Instead, our data indicate effects of fullerene C70 derivatives on viral genomic RNA packaging and HIV-1 cDNA synthesis during reverse transcription—without impairing reverse transcriptase activity though. Molecularly, this could be explained by a strong binding affinity of these fullerene derivatives to HIV-1 nucleocapsid domain, preventing its proper interaction with viral genomic RNA, thereby blocking reverse transcription and HIV-1 infectivity. Moreover, the fullerene derivatives’ oxidative activity and fluorescence quenching, which could be one of the reasons for the inconsistency among reported anti-HIV-1 mechanisms, are discussed herein.

Inhibition of HIV-1 by a Peptide Ligand of the Genomic RNA Packaging Signal Ψ

ChemMedChem ◽  
2008 ◽  
Vol 3 (5) ◽  
pp. 749-755 ◽  
Author(s):  
Julia Dietz ◽  
Joachim Koch ◽  
Ajit Kaur ◽  
Chinnappan Raja ◽  
Stefan Stein ◽  
...  
Keyword(s):  
Peptide Ligand ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Rna Packaging Signal ◽  
Hiv 1

scholarly journals MoMuLV and HIV-1 Nucleocapsid Proteins Have a Common Role in Genomic RNA Packaging but Different in Late Reverse Transcription

PLoS ONE ◽  
2012 ◽  
Vol 7 (12) ◽  
pp. e51534 ◽  
Author(s):  
Célia Chamontin ◽  
Bing Yu ◽  
Pierre-Jean Racine ◽  
Jena-Luc Darlix ◽  
Marylène Mougel
Keyword(s):  
Reverse Transcription ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Nucleocapsid Proteins ◽  
Hiv 1

scholarly journals An Intact TAR Element and Cytoplasmic Localization Are Necessary for Efficient Packaging of Human Immunodeficiency Virus Type 1 Genomic RNA

1999 ◽  
Vol 73 (5) ◽  
pp. 4127-4135 ◽  
Author(s):  
C. Helga-Maria ◽  
Marie-Louise Hammarskjöld ◽  
David Rekosh
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Splice Site ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Immunodeficiency Virus ◽  
Hiv 1 ◽  
Stem Structure

ABSTRACT Although most reports defining the human immunodeficiency virus type 1 (HIV-1) genomic RNA packaging signal have focused on the region downstream of the major 5′ splice site, others have suggested that sequences upstream of the splice site may also play an important role. In this study we have directly examined the role played by the HIV-1 TAR region in RNA packaging. For these experiments we used a proviral expression system that is largely independent of Tat for transcriptional activation. This allowed us to create constructs that efficiently expressed RNAs carrying mutations in TAR and to determine the ability of these RNAs to be packaged. Our results indicate that loss of sequences in TAR significantly reduce the ability of a viral RNA to be packaged. The requirement for TAR sequences in RNA packaging was further examined by using a series of missense mutations positioned throughout the entire TAR structure. TAR mutations previously shown to influence Tat transactivation, such as G31U in the upper loop region or UCU to AAG in the bulge (nucleotides [nt] 22 to 24), failed to have any effect on RNA packaging. Mutations which disrupted the portion of the TAR stem immediately below the bulge also had little effect. In contrast, dramatic effects on RNA packaging were observed with constructs containing mutations in the lower portion of the TAR stem. Point mutations which altered nt 5 to 9, 10 to 15, 44 to 49, or 50 to 54 all reduced RNA packaging 11- to 25-fold. However, compensatory double mutations which restored the stem structure were able to restore packaging. These results indicate that an intact lower stem structure, rather than a specific sequence, is required for RNA packaging. Our results also showed that RNA molecules retained within the nucleus cannot be packaged, unless they are transported to the cytoplasm by either Rev/Rev response element or the Mason-Pfizer monkey virus constitutive transport element.

scholarly journals A Heterologous, High-Affinity RNA Ligand for Human Immunodeficiency Virus Gag Protein Has RNA Packaging Activity

2000 ◽  
Vol 74 (1) ◽  
pp. 541-546 ◽  
Author(s):  
Jared L. Clever ◽  
Randy A. Taplitz ◽  
Michael A. Lochrie ◽  
Barry Polisky ◽  
Tristram G. Parslow
Keyword(s):  
Human Immunodeficiency Virus ◽  
Specific Binding ◽  
Single Point Mutation ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Gag Protein ◽  
High Affinity ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Retroviral RNA encapsidation depends on the specific binding of Gag proteins to packaging (ψ) 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 ψ 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 ψ 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.

scholarly journals An epitranscriptomic switch at the 5′-UTR controls genome selection during HIV-1 genomic RNA packaging

2019 ◽  
Author(s):  
Camila Pereira-Montecinos ◽  
Daniela Toro-Ascuy ◽  
Cecilia Rojas-Fuentes ◽  
Sebastián Riquelme-Barrios ◽  
Bárbara Rojas-Araya ◽  
...  
Keyword(s):  
Full Length ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Gag Protein ◽  
Rna Molecules ◽  
Viral Genomes ◽  
Viral Particles ◽  
Demethylase Activity ◽  
Retroviral Replication ◽  
Hiv 1

ABSTRACTDuring retroviral replication, the full-length RNA serves both as mRNA and genomic RNA (gRNA). While the simple retrovirus MLV segregates its full-length RNA into two functional populations, the HIV-1 full-length RNA was proposed to exist as a single population used indistinctly for protein synthesis or packaging. However, the mechanisms by which the HIV-1 Gag protein selects the two RNA molecules that will be packaged into nascent virions remain poorly understood. Here, we demonstrate that HIV-1 full-length RNA packaging is regulated through an epitranscriptomic switch requiring demethylation of two conserved adenosine residues present within the 5′-UTR. As such, while m6A deposition by METTL3/METTL14 onto the full-length RNA was associated with increased Gag synthesis and reduced packaging, FTO-mediated demethylation was required for the incorporation of the full-length RNA into viral particles. Interestingly, HIV-1 Gag associates with the RNA demethylase FTO in the nucleus and drives full-length RNA demethylation. Finally, the specific inhibition of the FTO RNA demethylase activity suppressed HIV-1 full-length RNA packaging. Together, our data propose a novel epitranscriptomic mechanism allowing the selection of the full-length RNA molecules that will be used as viral genomes.

scholarly journals High efficiency of HIV-1 genomic RNA packaging and heterozygote formation revealed by single virion analysis

2009 ◽  
Vol 106 (32) ◽  
pp. 13535-13540 ◽  
Author(s):  
J. Chen ◽  
O. Nikolaitchik ◽  
J. Singh ◽  
A. Wright ◽  
C. E. Bencsics ◽  
...  
Keyword(s):  
High Efficiency ◽  
Genomic Rna ◽  
Rna Packaging ◽  
Hiv 1
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