Evidence map›Paper›PMID 20719953›Full record

ArticleJournal of virology2010

Poxvirus complement control proteins are expressed on the cell surface through an intermolecular disulfide bridge with the viral A56 protein.

Brian C DeHaven, Natasha M Girgis, Yuhong Xiao, Paul N Hudson, Victoria A Olson, Inger K Damon, Stuart N Isaacs

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. A comprehensive review of monkeypox virus and mpox characteristics.Frontiers in cellular and infection microbiology · 2024
    Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Poxviruses and the evolution of host range and virulence.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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 1 country.

Brian C DeHavenUniversity of Pennsylvania School of Medicine, Department of Medicine, Division of Infectious Diseases, 502 Johnson Pavilion, Philadelphia, PA 19104-6073, USA.
Natasha M Girgis
Yuhong Xiao
Paul N Hudson
Victoria A Olson
Inger K Damon
Stuart N Isaacs
Centers for Disease Control and Prevention · USUniversity of Pennsylvania · US

Funding

Smallpox vaccine and vaccinia complement control proteinU01AI066333 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ISAACS, STUART N. · 2005 to 2009
$1.6M
NIAID NIH HHS AI-066333NIAID NIH HHS U01 AI066333
6 · The paper itself

Abstract

The vaccinia virus (VACV) complement control protein (VCP) is an immunomodulatory protein that is both secreted from and expressed on the surface of infected cells. Surface expression of VCP occurs though an interaction with the viral transmembrane protein A56 and is dependent on a free N-terminal cysteine of VCP. Although A56 and VCP have been shown to interact in infected cells, the mechanism remains unclear. To investigate if A56 is sufficient for surface expression, we transiently expressed VCP and A56 in eukaryotic cell lines and found that they interact on the cell surface in the absence of other viral proteins. Since A56 contains three extracellular cysteines, we hypothesized that one of the cysteines may be unpaired and could therefore form a disulfide bridge with VCP. To test this, we generated a series of A56 mutants in which each cysteine was mutated to a serine, and we found that mutation of cysteine 162 abrogated VCP cell surface expression. We also tested the ability of other poxvirus complement control proteins to bind to VACV A56. While the smallpox homolog of VCP is able to bind VACV A56, the ectromelia virus (ECTV) VCP homolog is only able to bind the ECTV homolog of A56, indicating that these proteins may have coevolved. Surface expression of poxvirus complement control proteins may have important implications in viral pathogenesis, as a virus that does not express cell surface VCP is attenuated in vivo. This suggests that surface expression of VCP may contribute to poxvirus pathogenesis.

Indexed as

Cell LineCell MembraneCysteineDisulfidesHumansMutagenesis, Site-DirectedPoxviridaeViral Proteinscomplement-control protein, Vaccinia virusCysteineDisulfidesViral Proteins

Identifiers

PMID20719953
PMCPMC2953161
OpenAlexW2172089701

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.