Evidence map›Paper›PMID 26712001›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

HIV-1 RNA genome dimerizes on the plasma membrane in the presence of Gag protein.

Jianbo Chen, Sheikh Abdul Rahman, Olga A Nikolaitchik, David Grunwald, Luca Sardo, Ryan C Burdick, Sergey Plisov, Edward Liang, Sheldon Tai, Vinay K Pathak and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 85 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Article
  3. Transcription start site heterogeneity controls MDA5 sensing of unspliced HIV-1 RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. The biased adenosine-rich content of the HIV-1 genome serves as a molecular signature that facilitates efficient packaging.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Proteomic Characterization of HIV Infection.Advances in experimental medicine and biology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Imaging HIV-1 Nuclear Import, Uncoating, and Proviral Transcription.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Jianbo ChenViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702; chenjia@mail.nih.gov wei-shau.hu@nih.gov.
Sheikh Abdul RahmanViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
Olga A NikolaitchikViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
David GrunwaldRNA Therapeutics Institute and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605;
Luca SardoViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
Ryan C BurdickViral Mutation Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702.
Sergey PlisovViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
Edward LiangViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
Sheldon TaiViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702;
Vinay K PathakViral Mutation Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702.
Wei-Shau HuViral Recombination Section, HIV Dynamics and Replication Program, National Cancer Institute at Frederick, Frederick, MD 21702; chenjia@mail.nih.gov wei-shau.hu@nih.gov.
National Cancer Institute · USColumbia University · USUniversity of Massachusetts Chan Medical School · US

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Structure and Function of Vif and APOBEC3 (A3) ProteinsZIABC010595 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PATHAK, VINAY K. · 2009 to 2025
$14.8M
Understanding Retroviral Gag and RNA Targeting and Virus AssemblyZIABC010506 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HU, WEI-SHAU · 2009 to 2025
$12.1M
Intramural NIH HHSNIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

Retroviruses package a dimeric genome comprising two copies of the viral RNA. Each RNA contains all of the genetic information for viral replication. Packaging a dimeric genome allows the recovery of genetic information from damaged RNA genomes during DNA synthesis and promotes frequent recombination to increase diversity in the viral population. Therefore, the strategy of packaging dimeric RNA affects viral replication and viral evolution. Although its biological importance is appreciated, very little is known about the genome dimerization process. HIV-1 RNA genomes dimerize before packaging into virions, and RNA interacts with the viral structural protein Gag in the cytoplasm. Thus, it is often hypothesized that RNAs dimerize in the cytoplasm and the RNA-Gag complex is transported to the plasma membrane for virus assembly. In this report, we tagged HIV-1 RNAs with fluorescent proteins, via interactions of RNA-binding proteins and motifs in the RNA genomes, and studied their behavior at the plasma membrane by using total internal reflection fluorescence microscopy. We showed that HIV-1 RNAs dimerize not in the cytoplasm but on the plasma membrane. Dynamic interactions occur among HIV-1 RNAs, and stabilization of the RNA dimer requires Gag protein. Dimerization often occurs at an early stage of the virus assembly process. Furthermore, the dimerization process is probably mediated by the interactions of two RNA-Gag complexes, rather than two RNAs. These findings advance the current understanding of HIV-1 assembly and reveal important insights into viral replication mechanisms.

Indexed as

DimerizationBacterial Proteinsbeta-GlobinsCell Membranegag Gene Products, Human Immunodeficiency VirusGenome, ViralHeLa CellsHIV-1HIV-2HumansLuminescent ProteinsMicroscopy, FluorescenceRNA, MessengerRNA TransportRNA, ViralStaining and LabelingBacterial Proteinsbeta-Globinsgag Gene Products, Human Immunodeficiency VirusLuminescent ProteinsRNA, MessengerRNA, Viralyellow fluorescent protein, BacteriaGag–RNA complexretrovirusRNA-binding proteinRNA genomevirus assembly

Identifiers

PMID26712001
PMCPMC4720333
OpenAlexW2208465122

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.