Evidence map›Paper›PMID 24093474›Full record

ArticleACS chemical biology2013

Scaffold properties are a key determinant of the size and shape of self-assembled virus-derived particles.

Stanislav Kler, Joseph Che-Yen Wang, Mary Dhason, Ariella Oppenheim, Adam Zlotnick

Abstract read
In one paragraph

Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Physical, chemical, and synthetic virology: Reprogramming viruses as controllable nanodevices.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Allosteric Control of Icosahedral Capsid Assembly.The journal of physical chemistry. B · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Mechanisms of virus assembly.Annual review of physical chemistry · 2015
    Review
  17. Pathways for virus assembly around nucleic acids.Journal of molecular biology · 2014
    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

5 authors.

Stanislav KlerDepartment of Hematology, Hebrew University-Hadassah Medical School , Jerusalem 91120, Israel.
Joseph Che-Yen Wang
Mary Dhason
Ariella Oppenheim
Adam Zlotnick

Funding

The Biophysics of Virus Capsid AssemblyR01AI077688 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2009 to 2013
$1.5M
NIAID NIH HHS R01 AI077688NIAID NIH HHS R01-AI077688
6 · The paper itself

Abstract

Controlling the geometry of self-assembly will enable a greater diversity of nanoparticles than now available. Viral capsid proteins, one starting point for investigating self-assembly, have evolved to form regular particles. The polyomavirus SV40 assembles from pentameric subunits and can encapsidate anionic cargos. On short ssRNA (≤814 nt), SV40 pentamers form 22 nm diameter capsids. On RNA too long to fit a T = 1 particle, pentamers forms strings of 22 nm particles and heterogeneous particles of 29-40 nm diameter. However, on dsDNA SV40 forms 50 nm particles composed of 72 pentamers. A 7.2-Å resolution cryo-EM image reconstruction of 22 nm particles shows that they are built of 12 pentamers arranged with T = 1 icosahedral symmetry. At 3-fold vertices, pentamers each contribute to a three-helix triangle. This geometry of interaction is not seen in crystal structures of T = 7 viruses and provides a structural basis for the smaller capsids. We propose that the heterogeneous particles are actually mosaics formed by combining different geometries of interaction from T = 1 capsids and virions. Assembly can be trapped in novel conformations because SV40 interpentamer contacts are relatively strong. The implication is that by virtue of their large catalog of interactions, SV40 pentamers have the ability to self-assemble on and conform to a broad range of shapes.

Indexed as

CapsidCapsid ProteinsCryoelectron MicroscopyCrystallography, X-RayDNAModels, MolecularMolecular ConformationNucleoproteinsParticle SizeRNA, Double-StrandedRNA, ViralSimian virus 40VirionCapsid ProteinsDNANucleoproteinsRNA, Double-StrandedRNA, Viral

Identifiers

PMID24093474
PMCPMC3870028

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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.