Evidence map›Paper›PMID 24257617›Full record

ArticleJournal of virology2014

Cryo-electron microscopy reconstruction shows poliovirus 135S particles poised for membrane interaction and RNA release.

Carmen Butan, David J Filman, James M Hogle

Abstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Detection methods targeting the positive- and negative-sense RNA transcripts from plus-stranded RNA viruses.APMIS : acta pathologica, microbiologica, et immunologica Scandinavica · 2022
    Article
  8. Article
  9. Manipulation of Host Cell Organelles by Intracellular Pathogens.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Hepatitis A Virus Capsid Structure.Cold Spring Harbor perspectives in medicine · 2019
    Review
  19. Article
  20. 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

3 authors.

Carmen ButanDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
David J Filman
James M Hogle

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Structural Analysis of Enterovirus Cell Entry PathwaysR01AI020566 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI HOGLE, JAMES M · 1985 to 2018
$9.0M
HIGH-RESOLUTION CRYSTALLOGRAPHIC STUDIES OF POLIOVIRUSR37AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 1992 to 2001
$934k
Structual Analysis of Enterovirus Cell Entry PathwaysR21AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 2002 to 2002
$258k
NIAID NIH HHS AI020566NIAID NIH HHS R01 AI020566NIAID NIH HHS R21 AI020566NIAID NIH HHS R37 AI020566NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41GM103310
6 · The paper itself

Abstract

During infection, binding of mature poliovirus to cell surface receptors induces an irreversible expansion of the capsid, to form an infectious cell-entry intermediate particle that sediments at 135S. In these expanded virions, the major capsid proteins (VP1 to VP3) adopt an altered icosahedral arrangement to open holes in the capsid at 2-fold and quasi-3-fold axes, and internal polypeptides VP4 and the N terminus of VP1, which can bind membranes, become externalized. Cryo-electron microscopy images for 117,330 particles were collected using Leginon and reconstructed using FREALIGN. Improved rigid-body positioning of major capsid proteins established reliably which polypeptide segments become disordered or rearranged. The virus-to-135S transition includes expansion of 4%, rearrangements of the GH loops of VP3 and VP1, and disordering of C-terminal extensions of VP1 and VP2. The N terminus of VP1 rearranges to become externalized near its quasi-3-fold exit, binds to rearranged GH loops of VP3 and VP1, and attaches to the top surface of VP2. These details improve our understanding of subsequent stages of infection, including endocytosis and RNA transfer into the cytoplasm.

Indexed as

CapsidCapsid ProteinsCell MembraneCryoelectron MicroscopyHumansPoliomyelitisPoliovirusProtein Structure, TertiaryRNA, ViralVirionCapsid ProteinsRNA, Viral

Identifiers

PMID24257617
PMCPMC3911577

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.