Evidence map›Paper›PMID 28711172›Full record

ArticleBiophysical journal2017

The Effect of RNA Secondary Structure on the Self-Assembly of Viral Capsids.

Christian Beren, Lisa L Dreesens, Katherine N Liu, Charles M Knobler, William M Gelbart

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Physics of viral dynamics.Nature reviews. Physics · 2021
    Review
  12. Virus Assembly Pathways: Straying Away but Not Too Far.Small (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  13. Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020
    Review
  14. Nonspherical Coacervate Shapes in an Enzyme-Driven Active System.Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. A modelling paradigm for RNA virus assembly.Current opinion in virology · 2018
    Review
  19. Laboratory evolution of virus-like nucleocapsids from nonviral protein cages.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. The effect of RNA stiffness on the self-assembly of virus particles.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    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 at 1 institution in 1 country.

Christian BerenDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Lisa L DreesensDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Katherine N LiuDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
Charles M KnoblerDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California. Electronic address: knobler@chem.ucla.edu.
William M GelbartDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, California.
University of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous work has shown that purified capsid protein (CP) of cowpea chlorotic mottle virus (CCMV) is capable of packaging both purified single-stranded RNA molecules of normal composition (comparable numbers of A, U, G, and C nucleobases) and of varying length and sequence, and anionic synthetic polymers such as polystyrene sulfonate. We find that CCMV CP is also capable of packaging polyU RNAs, which-unlike normal-composition RNAs-do not form secondary structures and which act as essentially structureless linear polymers. Following our canonical two-step assembly protocol, polyU RNAs ranging in length from 1000 to 9000 nucleotides (nt) are completely packaged. Surprisingly, negative-stain electron microscopy shows that all lengths of polyU are packaged into 22-nm-diameter particles despite the fact that CCMV CP prefers to form 28-nm-diameter (T = 3) particles when packaging normal-composition RNAs. PolyU RNAs >5000 nt in length are packaged into multiplet capsids, in which a single RNA molecule is shared between two or more 22-nm-diameter capsids, in analogy with the multiplets of 28-nm-diameter particles formed with normal-composition RNAs >5000 nt long. Experiments in which viral RNA competes for viral CP with polyUs of equal length show that polyU, despite its lack of secondary structure, is packaged more efficiently than viral RNA. These findings illustrate that the secondary structure of the RNA molecule-and its absence-plays an essential role in determining capsid structure during the self-assembly of CCMV-like particles.

Indexed as

Nucleic Acid ConformationRNA, ViralVirus AssemblyBromovirusCapsidCapsid ProteinsElectrophoretic Mobility Shift AssayMicroscopy, Electron, TransmissionCapsid ProteinsRNA, Viral

Identifiers

PMID28711172
PMCPMC5529328
OpenAlexW2736181214

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.