Evidence map›Paper›PMID 19244330›Full record

ArticleJournal of virology2009

Mitochondrion-enriched anionic phospholipids facilitate flock house virus RNA polymerase membrane association.

Kenneth A Stapleford, Doron Rapaport, David J Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Review
  3. RNA virus replication depends on enrichment of phosphatidylethanolamine at replication sites in subcellular membranes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  4. Article
  5. Article
  6. Article
  7. Viruses and antiviral immunity in Drosophila.Developmental and comparative immunology · 2014
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 2 countries.

Kenneth A StaplefordUniversity of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Doron Rapaport
David J Miller
University of Michigan–Ann Arbor · USUniversity of Tübingen · DE

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
Virus-host interactions in replication complex assemblyR01AI062749 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MILLER, DAVID J · 2005 to 2009
$1.4M
NIAID NIH HHS R01 AI062749NIAID NIH HHS R01-AI062749NIGMS NIH HHS T32 GM007315NIGMS NIH HHS T32-GM007315
6 · The paper itself

Abstract

One characteristic of all positive-strand RNA viruses is the necessity to assemble viral RNA replication complexes on host intracellular membranes, a process whose molecular details are poorly understood. To study viral replication complex assembly we use the established model system of Flock House virus (FHV), which assembles its replication complexes on the mitochondrial outer membrane. The FHV RNA-dependent RNA polymerase, protein A, is the only viral protein necessary for genome replication in the budding yeast Saccharomyces cerevisiae. To examine the host components involved in protein A-membrane interactions, an initial step of FHV RNA replication complex assembly, we established an in vitro protein A membrane association assay. Protein A translated in vitro rapidly and specifically associated with mitochondria isolated from yeast, insect, and mammalian cells. This process was temperature dependent but independent of protease-sensitive mitochondrial outer membrane components or the host mitochondrial import machinery. Furthermore, lipid-binding studies revealed that protein A preferentially bound to specific anionic phospholipids, in particular the mitochondrion-specific phospholipid cardiolipin. These studies implicate membrane phospholipids as important host determinants for FHV RNA polymerase membrane association and provide evidence for the involvement of host phospholipids in positive-strand RNA virus membrane-specific targeting.

Indexed as

AnionsCell MembraneDNA-Directed RNA PolymerasesMembrane ProteinsMitochondriaNodaviridaePhospholipidsPorosityProtein BindingProtein TransportReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeStaphylococcal Protein ASubstrate SpecificityAnionsDNA-Directed RNA PolymerasesMembrane ProteinsPhospholipidsReceptors, Cytoplasmic and NuclearStaphylococcal Protein A

Identifiers

PMID19244330
PMCPMC2668453
OpenAlexW2114306688

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.