Evidence map›Paper›PMID 23918407›Full record

ArticleThe Journal of general virology2013

A virus-encoded potassium ion channel is a structural protein in the chlorovirus Paramecium bursaria chlorella virus 1 virion.

Giulia Romani, Adrianna Piotrowski, Stefan Hillmer, James Gurnon, James L Van Etten, Anna Moroni, Gerhard Thiel, Brigitte Hertel

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Chloroviruses.Viruses · 2019
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. 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

8 authors at 5 institutions in 4 countries.

Giulia RomaniDipartimento di Bioscienze, Università degli Studi di Milano e Istituto di Biofisica, CNR, Milano, Italy.
Adrianna PiotrowskiMembrane Biophysics Group, Department of Biology, Technical University Darmstadt, Germany.
Stefan HillmerCOS - Entwicklungsbiologie der Pflanzen, University of Heidelberg, Germany.
James GurnonDepartment of Plant Pathology and Nebraska Center for Virology, University of Nebraska, Lincoln, NE 68583-0900, USA.
James L Van EttenDepartment of Plant Pathology and Nebraska Center for Virology, University of Nebraska, Lincoln, NE 68583-0900, USA.
Anna MoroniDipartimento di Bioscienze, Università degli Studi di Milano e Istituto di Biofisica, CNR, Milano, Italy.
Gerhard ThielMembrane Biophysics Group, Department of Biology, Technical University Darmstadt, Germany.
Brigitte HertelMembrane Biophysics Group, Department of Biology, Technical University Darmstadt, Germany.
Technical University of Darmstadt · DEUniversity of Nebraska–Lincoln · USHeidelberg University · DEInstituto Biofisika · ESUniversity of Milan · IT

Funding

VIRAL SHUTOFF OF HOST TRANSCRIPTION--PBCV-1 INFECTEDP20RR015635 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI WOOD, CHARLES · 2000 to 2009
$22.1M
NCRR NIH HHS P20 RR015635NCRR NIH HHS P20-RR15635
6 · The paper itself

Abstract

Most chloroviruses encode small K(+) channels, which are functional in electrophysiological assays. The experimental finding that initial steps in viral infection exhibit the same sensitivity to channel inhibitors as the viral K(+) channels has led to the hypothesis that the channels are structural proteins located in the internal membrane of the virus particles. This hypothesis was questioned recently because proteomic studies failed to detect the channel protein in virions of the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1). Here, we used a mAb raised against the functional K(+) channel from chlorovirus MA-1D to search for the viral K(+) channel in the virus particle. The results showed that the antibody was specific and bound to the tetrameric channel on the extracellular side. The antibody reacted in a virus-specific manner with protein extracts from chloroviruses that encoded channels similar to that from MA-1D. There was no cross-reactivity with chloroviruses that encoded more diverse channels or with a chlorovirus that lacked a K(+) channel gene. Together with electron microscopic imaging, which revealed labelling of individual virus particles with the channel antibody, these results establish that the viral particles contain an active K(+) channel, presumably located in the lipid membrane that surrounds the DNA in the mature virions.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalChlorocebus aethiopsCOS CellsMiceMicroscopy, ElectronMolecular Sequence DataParameciumPhycodnaviridaePotassium ChannelsProteomicsViral Structural ProteinsVirionAntibodies, MonoclonalPotassium ChannelsViral Structural Proteins

Identifiers

PMID23918407
PMCPMC4093784
OpenAlexW2167591209

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.