Evidence map›Paper›PMID 22875972›Full record

ArticleJournal of virology2012

Vaccinia virus virion membrane biogenesis protein A11 associates with viral membranes in a manner that requires the expression of another membrane biogenesis protein, A6.

Xiang Wu, Xiangzhi Meng, Bo Yan, Lloyd Rose, Junpeng Deng, 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  3. Review
  4. Article
  5. 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
  6. Article
  7. 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
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 2 institutions in 1 country.

Xiang WuDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA.
Xiangzhi Meng
Bo Yan
Lloyd Rose
Junpeng Deng
Yan Xiang
The University of Texas Health Science Center at San Antonio · USOklahoma State University · US

Funding

Poxvirus Immune Evasion MechanismsR01AI079217 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2008 to 2018
$3.3M
Structure-function studies on IL-18, IL-18 binding proteins and receptorsR01AI081928 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI DENG, JUNPENG · 2009 to 2012
$1.3M
NIAID NIH HHS AI079217NIAID NIH HHS AI081928NIAID NIH HHS R01 AI079217NIAID NIH HHS R01 AI081928
6 · The paper itself

Abstract

A group of vaccinia virus (VACV) proteins, including A11, L2, and A6, are required for biogenesis of the primary envelope of VACV, specifically, for the acquisition of viral membrane precursors. However, the interconnection among these proteins is unknown and, with the exception of L2, the connection of these proteins with membranes is also unknown. In this study, prompted by the findings that A6 coprecipitated A11 and that the cellular distribution of A11 was dramatically altered by repression of A6 expression, we studied the localization of A11 in cells by using immunofluorescence and cell fractionation analysis. A11 was found to associate with membranes and colocalize with virion membrane proteins in viral replication factories during normal VACV replication. A11 partitioned almost equally between the detergent and aqueous phases upon Triton X-114 phase separation, demonstrating an intrinsic affinity with lipids. However, in the absence of infection or VACV late protein synthesis, A11 did not associate with cellular membranes. Furthermore, when A6 expression was repressed, A11 did not colocalize with any viral membrane proteins or associate with membranes. In contrast, when virion envelope formation was blocked at a later step by repression of A14 expression or by rifampin treatment, A11 colocalized with virion membrane proteins in the factories. Altogether, our data showed that A11 associates with viral membranes during VACV replication, and this association requires A6 expression. This study provides a physical connection between A11 and viral membranes and suggests that A6 regulates A11 membrane association.

Indexed as

AnimalsCell Line, TumorCell MembraneCricetinaeHEK293 CellsHeLa CellsHumansProtein BindingRifampinVaccinia virusViral Matrix ProteinsVirus AssemblyVirus ReplicationRifampinViral Matrix Proteins

Identifiers

PMID22875972
PMCPMC3457167
OpenAlexW2078984921

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.