Evidence map›Paper›PMID 25486587›Full record

ArticleVirology2015

Fine structure of the vaccinia virion determined by controlled degradation and immunolocalization.

Nissin Moussatche, Richard C Condit

Open access · greenAbstract read
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structure of the poxvirus core.Nature structural & molecular biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  11. Article
  12. Article
  13. Surprisingly Effective Priming of CD8Journal of virology · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

Nissin MoussatcheDepartment of Molecular Genetics and Microbiology, University of Florida, Gainesville, FL 32610, USA. Electronic address: nissin@ufl.edu.
Richard C ConditDepartment of Molecular Genetics and Microbiology, University of Florida, Gainesville, FL 32610, USA.
University of Florida · US

Funding

Vaccinia Virus Genetics and MorphogenesisR01AI055560 · NIAID · UNIVERSITY OF FLORIDA · PI CONDIT, RICHARD C · 2004 to 2014
$3.2M
Vaccinia Virus Genetics and MorphogenesisR21AI055560 · NIAID · UNIVERSITY OF FLORIDA · PI CONDIT, RICHARD C · 2003 to 2003
$290k
NIAID NIH HHS R01 AI055560NIAID NIH HHS R01AI055560NIAID NIH HHS R21 AI055560
6 · The paper itself

Abstract

The vaccinia virion is a membraned, slightly flattened, barrel-shaped particle, with a complex internal structure featuring a biconcave core flanked by lateral bodies. Although the architecture of the purified mature virion has been intensely characterized by electron microscopy, the distribution of the proteins within the virion has been examined primarily using biochemical procedures. Thus, it has been shown that non-ionic and ionic detergents combined or not with a sulfhydryl reagent can be used to disrupt virions and, to a limited degree, separate the constituent proteins in different fractions. Applying a controlled degradation technique to virions adsorbed on EM grids, we were able to immuno-localize viral proteins within the virion particle. Our results show after NP40 and DTT treatment, membrane proteins are removed from the virion surface revealing proteins that are associated with the lateral bodies and the outer layer of the core wall. Combined treatment using high salt and high DTT removed lateral body proteins and exposed proteins of the internal core wall. Cores treated with proteases could be disrupted and the internal components were exposed. Cts8, a mutant in the A3 protein, produces aberrant virus that, when treated with NP-40 and DTT, releases to the exterior the virus DNA associated with other internal core proteins. With these results, we are able to propose a model for the structure the vaccinia virion.

Indexed as

Gene Expression Regulation, ViralImmunohistochemistryMutationPeptide HydrolasesProteolysisStaining and LabelingVaccinia virusViral Envelope ProteinsVirionVirus AssemblyPeptide HydrolasesViral Envelope ProteinsControlled degradationImmunolocalization of proteinsVaccinia virusVirion structure

Identifiers

PMID25486587
PMCPMC4280304
OpenAlexW2008398620

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.