Evidence map›Paper›PMID 32104873›Full record

ArticleSoft matter2020

pH stability and disassembly mechanism of wild-type simian virus 40.

Roi Asor, Daniel Khaykelson, Orly Ben-Nun-Shaul, Yael Levi-Kalisman, Ariella Oppenheim, Uri Raviv

Open access · greenAbstract read
In one paragraph

Article in Soft matter, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Highly stableFrontiers in bioengineering and biotechnology · 2024
    Article
  8. Upgrade ofJournal of applied crystallography · 2023
    Article
  9. Mechanism of Tubulin Oligomers and Single-Ring Disassembly Catastrophe.The journal of physical chemistry letters · 2022
    Article
  10. Hybrid Nanoassemblies from Viruses and DNA Nanostructures.Nanomaterials (Basel, Switzerland) · 2021
    Review
  11. Review
  12. Multivalent ions and biomolecules: Attempting a comprehensive perspective.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020
    Review
  13. Article
  14. Article
  15. Review
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

6 authors at 2 institutions in 4 countries.

Roi AsorInstitute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem 9190401, Israel. uri.raviv@mail.huji.ac.il.
Daniel Khaykelson
Orly Ben-Nun-Shaul
Yael Levi-Kalisman
Ariella Oppenheim
Uri Raviv
Hebrew University of Jerusalem · ILHadassah · US

Funding

Computational modeling of viral capsid and bacterial microcompartment assemblyR01GM108021 · NIGMS · BRANDEIS UNIVERSITY · PI HAGAN, MICHAEL F · 2013 to 2021
$2.7M
NIGMS NIH HHS R01 GM108021
6 · The paper itself

Abstract

Viruses are remarkable self-assembled nanobiomaterial-based machines, exposed to a wide range of pH values. Extreme pH values can induce dramatic structural changes, critical for the function of the virus nanoparticles, including assembly and genome uncoating. Tuning cargo-capsid interactions is essential for designing virus-based delivery systems. Here we show how pH controls the structure and activity of wild-type simian virus 40 (wtSV40) and the interplay between its cargo and capsid. Using cryo-TEM and solution X-ray scattering, we found that wtSV40 was stable between pH 5.5 and 9, and only slightly swelled with increasing pH. At pH 3, the particles aggregated, while capsid protein pentamers continued to coat the virus cargo but lost their positional correlations. Infectivity was only partly lost after the particles were returned to pH 7. At pH 10 or higher, the particles were unstable, lost their infectivity, and disassembled. Using time-resolved experiments we discovered that disassembly began by swelling of the particles, poking a hole in the capsid through which the genetic cargo escaped, followed by a slight shrinking of the capsids and complete disassembly. These findings provide insight into the fundamental intermolecular forces, essential for SV40 function, and for designing virus-based nanobiomaterials, including delivery systems and antiviral drugs.

Indexed as

Capsid ProteinsGenome, ViralHumansHydrogen-Ion ConcentrationModels, MolecularNanoparticlesSimian virus 40Capsid Proteins

Identifiers

PMID32104873
PMCPMC7189960
OpenAlexW3004640237

What OpenQuestion holds

Textmetadata
LicenceTDM
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.