Evidence map›Paper›PMID 22398288›Full record

ArticleJournal of virology2012

Vaccinia virus A6 is essential for virion membrane biogenesis and localization of virion membrane proteins to sites of virion assembly.

Xiangzhi Meng, Addie Embry, Lloyd Rose, Bo Yan, Chungui Xu, Yan Xiang

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. 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
1.3field-weighted citation impact, top 21% 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, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Enigmatic origin of the poxvirus membrane from the endoplasmic reticulum shown by 3D imaging of vaccinia virus assembly mutants.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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 1 institution in 1 country.

Xiangzhi MengDepartment of Microbiology and Immunology, The University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA.
Addie Embry
Lloyd Rose
Bo Yan
Chungui Xu
Yan Xiang
The University of Texas Health Science Center at San Antonio · US

Funding

Poxvirus Immune Evasion MechanismsR01AI079217 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2008 to 2018
$3.3M
NIAID NIH HHS AI079217NIAID NIH HHS R01 AI079217
6 · The paper itself

Abstract

Poxvirus acquires its primary envelope through a process that is distinct from those of other enveloped viruses. The molecular mechanism of this process is poorly understood, but several poxvirus proteins essential for the process have been identified in studies of vaccinia virus (VACV), the prototypical poxvirus. Previously, we identified VACV A6 as an essential factor for virion morphogenesis by studying a temperature-sensitive mutant with a lesion in A6. Here, we further studied A6 by constructing and characterizing an inducible virus (iA6) that could more stringently repress A6 expression. When A6 expression was induced by the inducer isopropyl-β-D-thiogalactoside (IPTG), iA6 replicated normally, and membrane proteins of mature virions (MVs) predominantly localized in viral factories where virions were assembled. However, when A6 expression was repressed, electron microscopy of infected cells showed the accumulation of large viroplasm inclusions containing virion core proteins but no viral membranes. Immunofluorescence and cell fractionation studies showed that the major MV membrane proteins A13, A14, D8, and H3 did not localize to viral factories but instead accumulated in the secretory compartments, including the endoplasmic reticulum. Overall, our results show that A6 is an additional VACV protein that participates in an early step of virion membrane biogenesis. Furthermore, A6 is required for MV membrane protein localization to sites of virion assembly, suggesting that MV membrane proteins or precursors of MV membranes are trafficked to sites of virion assembly through an active, virus-mediated process that requires A6.

Indexed as

Virus AssemblyCell MembraneHumansProtein TransportVacciniaVaccinia virusViral Core ProteinsViral Envelope ProteinsVirionViral Core ProteinsViral Envelope Proteins

Identifiers

PMID22398288
PMCPMC3347295
OpenAlexW2164912261

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.