Evidence map›Paper›PMID 29114055›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Immature HIV-1 lattice assembly dynamics are regulated by scaffolding from nucleic acid and the plasma membrane.

Alexander J Pak, John M A Grime, Prabuddha Sengupta, Antony K Chen, Aleksander E P Durumeric, Anand Srivastava, Mark Yeager, John A G Briggs, Jennifer Lippincott-Schwartz, Gregory A Voth

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Mechanistic Insights into HIV-1 Capsid Interactions with CPSF6.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1The journal of physical chemistry. B · 2026
    Article
  5. Article
  6. Membrane bending energy selects for compact growth of protein assemblies.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  12. Article
  13. Article
  14. The "basics" of HIV-1 assembly.PLoS pathogens · 2024
    Article
  15. HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. OpenMSCG: A Software Tool for Bottom-Up Coarse-Graining.The journal of physical chemistry. B · 2023
    Article
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

10 authors at 6 institutions in 5 countries.

Alexander J PakDepartment of Chemistry, The University of Chicago, Chicago, IL 60637.
John M A GrimeDepartment of Chemistry, The University of Chicago, Chicago, IL 60637.
Prabuddha SenguptaHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147.
Antony K ChenEunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Aleksander E P DurumericDepartment of Chemistry, The University of Chicago, Chicago, IL 60637.
Anand SrivastavaMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Mark YeagerDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22903.
John A G BriggsMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Jennifer Lippincott-SchwartzHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA 20147.
Gregory A VothDepartment of Chemistry, The University of Chicago, Chicago, IL 60637; gavoth@uchicago.edu.
University of Chicago · USJanelia Research Campus · USIndian Institute of Science Bangalore · INMRC Laboratory of Molecular Biology · GBNational Institutes of Health · USUniversity of Virginia Health System · US

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Howard Hughes Medical InstituteMedical Research Council MC_UP_1201/16NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

The packaging and budding of Gag polyprotein and viral RNA is a critical step in the HIV-1 life cycle. High-resolution structures of the Gag polyprotein have revealed that the capsid (CA) and spacer peptide 1 (SP1) domains contain important interfaces for Gag self-assembly. However, the molecular details of the multimerization process, especially in the presence of RNA and the cell membrane, have remained unclear. In this work, we investigate the mechanisms that work in concert between the polyproteins, RNA, and membrane to promote immature lattice growth. We develop a coarse-grained (CG) computational model that is derived from subnanometer resolution structural data. Our simulations recapitulate contiguous and hexameric lattice assembly driven only by weak anisotropic attractions at the helical CA-SP1 junction. Importantly, analysis from CG and single-particle tracking photoactivated localization (spt-PALM) trajectories indicates that viral RNA and the membrane are critical constituents that actively promote Gag multimerization through scaffolding, while overexpression of short competitor RNA can suppress assembly. We also find that the CA amino-terminal domain imparts intrinsic curvature to the Gag lattice. As a consequence, immature lattice growth appears to be coupled to the dynamics of spontaneous membrane deformation. Our findings elucidate a simple network of interactions that regulate the early stages of HIV-1 assembly and budding.

Indexed as

Binding SitesCell MembraneGene ExpressionGene Products, gagHEK293 CellsHIV-1Host-Pathogen InteractionsHumansKineticsMolecular Dynamics SimulationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryRecombinant ProteinsRNA, ViralGene Products, gagRecombinant ProteinsRNA, ViralCA–SP1 junctioncoarse-grained molecular dynamicsGagHIV packaging and buddingself-assembly

Identifiers

PMID29114055
PMCPMC5703280
OpenAlexW2734451627

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.