Evidence map›Paper›PMID 21931553›Full record

ArticlePLoS pathogens2011

Membrane remodeling by the double-barrel scaffolding protein of poxvirus.

Jae-Kyung Hyun, Cathy Accurso, Marcel Hijnen, Philipp Schult, Anne Pettikiriarachchi, Alok K Mitra, Fasséli Coulibaly

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

39 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Cellular homologs of the double jelly-roll major capsid proteins clarify the origins of an ancient virus kingdom.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. Global Organization and Proposed Megataxonomy of the Virus World.Microbiology and molecular biology reviews : MMBR · 2020
    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

7 authors at 2 institutions in 2 countries.

Jae-Kyung HyunSchool of Biological Sciences, the University of Auckland, Auckland, New Zealand.
Cathy Accurso
Marcel Hijnen
Philipp Schult
Anne Pettikiriarachchi
Alok K Mitra
Fasséli Coulibaly
Monash University · AUUniversity of Auckland · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 Å crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.

Indexed as

CapsidCapsid ProteinsCrystallography, X-RayLiposomesMembranes, ArtificialMicroscopy, ElectronModels, MolecularProtein Structure, TertiaryVaccinia virusVirus AssemblyCapsid ProteinsLiposomesMembranes, Artificial

Identifiers

PMID21931553
PMCPMC3169552
OpenAlexW2005618401

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.