ArticleRetrovirology2016
Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling.
Article in Retrovirology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 28 citations in OpenAlex.
- Human RPL7 and DDX21 function synergistically with HTLV-1 Gag to overcome genomic RNA structural barriers that block tRNAPro primer annealing.Nucleic acids research · 2026Article
- Hijacking the Host: Post-Translational Modifications as Molecular Switches in HIV Persistence and Immune Evasion.Journal of medical virology · 2026Review
- Transcriptomic and flavor metabolomic exploration of the genetic basis of meat quality and flavor in Tibetan sheep.BMC genomics · 2025Article
- Structural flexibility in the ordered domain of the dengue virus strain 2 capsid protein is critical for chaperoning viral RNA replication.Cellular and molecular life sciences : CMLS · 2025Article
- Tracking HIV persistence across T cell lineages during early ART-treated HIV-1-infection using a reservoir-marking humanized mouse model.Nature communications · 2025Article
- The Influence of Extra-Ribosomal Functions of Eukaryotic Ribosomal Proteins on Viral Infection.Biomolecules · 2024Review
- Retroviral PBS-segment sequence and structure: Orchestrating early and late replication events.Retrovirology · 2024Review
- The human cellular protein NoL12 is a specific partner of the HIV-1 nucleocapsid protein NCp7.Journal of virology · 2023Article
- Article
- RPLP1, an NS4B-interacting protein, enhances production of CSFV through promoting translation of viral genome.Virulence · 2022Article
- Genome-wide CRISPR screens identify combinations of candidate latency reversing agents for targeting the latent HIV-1 reservoir.Science translational medicine · 2022Article
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- Monte Carlo Simulation of the Efficiency of Fluorescence Resonance Energy Transfer, FRET Phenomenon.Journal of fluorescence · 2022Article
- Selective regulation in ribosome biogenesis and protein production for efficient viral translation.Archives of microbiology · 2021Review
- Fatal attraction: The roles of ribosomal proteins in the viral life cycle.Wiley interdisciplinary reviews. RNA · 2021Review
- The Effect of Interferons on Presentation of Defective Ribosomal Products as HLA Peptides.Molecular & cellular proteomics : MCP · 2021Article
- The nucleic acid chaperone activity of the HIV-1 Gag polyprotein is boosted by its cellular partner RPL7: a kinetic study.Nucleic acids research · 2020Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Significant Differences in RNA Structure Destabilization by HIV-1 GagDp6 and NCp7 Proteins.Viruses · 2020Article
- Ribosomal Protein L13 Promotes IRES-Driven Translation of Foot-and-Mouth Disease Virus in a Helicase DDX3-Dependent Manner.Journal of virology · 2020Article
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn HIV-1 infected cells, the integrated viral DNA is transcribed by the host cell machinery to generate the full length HIV-1 RNA (FL RNA) that serves as mRNA encoding for the Gag and GagPol precursors. Virion formation is orchestrated by Gag, and the current view is that a specific interaction between newly made Gag molecules and FL RNA initiates the process. This in turn would cause FL RNA dimerization by the NC domain of Gag (GagNC). However the RNA chaperoning activity of unprocessed Gag is low as compared to the mature NC protein. This prompted us to search for GagNC co-factors.
resultsHere we report that RPL7, a major ribosomal protein involved in translation regulation, is a partner of Gag via its interaction with the NC domain. This interaction is mediated by the NC zinc fingers and the N- and C-termini of RPL7, respectively, but seems independent of RNA binding, Gag oligomerization and its interaction with the plasma membrane. Interestingly, RPL7 is shown for the first time to exhibit a potent DNA/RNA chaperone activity higher than that of Gag. In addition, Gag and RPL7 can function in concert to drive rapid nucleic acid hybridization.
conclusionsOur results show that GagNC interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly.
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