Evidence map›Paper›PMID 30301857›Full record

ArticlemBio2018

Staufen1 Interacts with Multiple Components of the Ebola Virus Ribonucleoprotein and Enhances Viral RNA Synthesis.

Jingru Fang, Colette Pietzsch, Palaniappan Ramanathan, Rodrigo I Santos, Philipp A Ilinykh, Mariano A Garcia-Blanco, Alexander Bukreyev, Shelton S Bradrick

Open access · goldAbstract read
In one paragraph

Article in mBio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Proximity interactome analysis of Lassa polymerase reveals eRF3a/GSPT1 as a druggable target for host-directed antivirals.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 2 countries.

Jingru FangDepartment of Biochemistry & Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA.
Colette PietzschDepartment of Pathology, University of Texas Medical Branch, Galveston, Texas, USA.
Palaniappan RamanathanDepartment of Pathology, University of Texas Medical Branch, Galveston, Texas, USA.
Rodrigo I SantosDepartment of Pathology, University of Texas Medical Branch, Galveston, Texas, USA.
Philipp A IlinykhDepartment of Pathology, University of Texas Medical Branch, Galveston, Texas, USA.
Mariano A Garcia-BlancoDepartment of Biochemistry & Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA maragarc@utmb.edu alexander.bukreye@utmb.edu ssbradri@utmb.edu.
Alexander BukreyevDepartment of Pathology, University of Texas Medical Branch, Galveston, Texas, USA maragarc@utmb.edu alexander.bukreye@utmb.edu ssbradri@utmb.edu.
Shelton S BradrickDepartment of Biochemistry & Molecular Biology, University of Texas Medical Branch, Galveston, Texas, USA maragarc@utmb.edu alexander.bukreye@utmb.edu ssbradri@utmb.edu.
The University of Texas Medical Branch at Galveston · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ebola virus (EBOV) genome and mRNAs contain long, structured regions that could hijack host RNA-binding proteins to facilitate infection. We performed RNA affinity chromatography coupled with mass spectrometry to identify host proteins that bind to EBOV RNAs and identified four high-confidence proviral host factors, including Staufen1 (STAU1), which specifically binds both 3' and 5' extracistronic regions of the EBOV genome. We confirmed that EBOV infection rate and production of infectious particles were significantly reduced in STAU1-depleted cells. STAU1 was recruited to sites of EBOV RNA synthesis upon infection and enhanced viral RNA synthesis. Furthermore, STAU1 interacts with EBOV nucleoprotein (NP), virion protein 30 (VP30), and VP35; the latter two bridge the viral polymerase to the NP-coated genome, forming the viral ribonucleoprotein (RNP) complex. Our data indicate that STAU1 plays a critical role in EBOV replication by coordinating interactions between the viral genome and RNA synthesis machinery.

Indexed as

Host-Pathogen InteractionsCell LineCytoskeletal ProteinsEbolavirusGenome, ViralHumansProtein BindingRibonucleoproteinsRNA-Binding ProteinsRNA, ViralTranscription FactorsViral ProteinsViral Regulatory and Accessory ProteinsCytoskeletal ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, ViralSTAU1 protein, humanTranscription FactorsViral ProteinsViral Regulatory and Accessory ProteinsVP30 protein, ebola virusVP35 protein, filovirusebola virusRNA binding proteinsRNA replicationvirus-host interactions

Identifiers

PMID30301857
PMCPMC6178623
OpenAlexW2897429651

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.