Evidence map›Paper›PMID 24109217›Full record

ArticleJournal of virology2013

A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition.

Paul W Keller, Rick K Huang, Matthew R England, Kayoko Waki, Naiqian Cheng, J Bernard Heymann, Rebecca C Craven, Eric O Freed, Alasdair C Steven

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.4field-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

54 citing papers in PubMed, 71 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Article
  3. Article
  4. Review
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  6. Article
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  8. Article
  9. Review
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  12. High resolution electron tomography and segmentation-by-modeling interpretation in Bsoft.Protein science : a publication of the Protein Society · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Maturation of retroviruses.Current opinion in virology · 2019
    Review
  18. Structure of the Ty3/Gypsy retrotransposon capsid and the evolution of retroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Review
  20. 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

9 authors at 4 institutions in 1 country.

Paul W KellerLaboratory of Structural Biology Research, National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Rick K Huang
Matthew R England
Kayoko Waki
Naiqian Cheng
J Bernard Heymann
Rebecca C Craven
Eric O Freed
Alasdair C Steven
National Institutes of Health · USNational Cancer Institute · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · USPennsylvania State University · US

Funding

Inhibition of HIV-1 MaturationZIABC010778 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2009 to 2025
$9.7M
Structural Biology Of Retrovirus AssemblyZIAAR041166 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 2009 to 2020
$9.2M
VIRUSES AND CANCERT32CA060395 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MEYERS, CRAIG M · 1994 to 2021
$4.3M
Interactions of the CA Protein in the Retrovirus CoreR01CA100322 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI CRAVEN, REBECCA C. · 2003 to 2013
$2.5M
Intramural NIH HHSNCI NIH HHS 2 T32 CA60395NCI NIH HHS CA100322NCI NIH HHS R01 CA100322NCI NIH HHS T32 CA060395
6 · The paper itself

Abstract

Retrovirus maturation involves sequential cleavages of the Gag polyprotein, initially arrayed in a spherical shell, leading to formation of capsids with polyhedral or conical morphology. Evidence suggests that capsids assemble de novo inside maturing virions from dissociated capsid (CA) protein, but the possibility persists of a displacive pathway in which the CA shell remains assembled but is remodeled. Inhibition of the final cleavage between CA and spacer peptide SP1/SP blocks the production of mature capsids. We investigated whether retention of SP might render CA assembly incompetent by testing the ability of Rous sarcoma virus (RSV) CA-SP to assemble in vitro into icosahedral capsids. Capsids were indeed assembled and were indistinguishable from those formed by CA alone, indicating that SP was disordered. We also used cryo-electron tomography to characterize HIV-1 particles produced in the presence of maturation inhibitor PF-46396 or with the cleavage-blocking CA5 mutation. Inhibitor-treated virions have a shell that resembles the CA layer of the immature Gag shell but is less complete. Some CA protein is generated but usually not enough for a mature core to assemble. We propose that inhibitors like PF-46396 bind to the Gag lattice where they deny the protease access to the CA-SP1 cleavage site and prevent the release of CA. CA5 particles, which exhibit no cleavage at the CA-SP1 site, have spheroidal shells with relatively thin walls. It appears that this lattice progresses displacively toward a mature-like state but produces neither conical cores nor infectious virions. These observations support the disassembly-reassembly pathway for core formation.

Indexed as

CapsidCapsid Proteinsgag Gene Products, Human Immunodeficiency VirusGene Products, gagHIV-1HumansModels, MolecularMutationRous sarcoma virusCapsid Proteinsgag Gene Products, Human Immunodeficiency VirusGene Products, gag

Identifiers

PMID24109217
PMCPMC3838239
OpenAlexW2145652748

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.