Evidence map›Paper›PMID 31634467›Full record

ArticleJournal of molecular biology2019

The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality.

Nathan E Jespersen, Cedric Leyrat, Francine C Gérard, Jean-Marie Bourhis, Danielle Blondel, Marc Jamin, Elisar Barbar

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2019. 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
1.8field-weighted citation impact, top 16% 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, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Structural insights into the multifunctionality of rabies virus P3 protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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 3 institutions in 2 countries.

Nathan E JespersenFrom the Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.
Cedric LeyratInstitut de Génomique Fonctionnelle, CNRS UMR-5203 INSERM U1191, University of Montpellier, Montpellier, France.
Francine C GérardUniversité Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000, Grenoble, France.
Jean-Marie BourhisUniversité Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000, Grenoble, France.
Danielle BlondelInstitut de Biologie Intégrative de La Cellule (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette Cedex, France.
Marc JaminUniversité Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000, Grenoble, France.
Elisar BarbarFrom the Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA. Electronic address: barbare@oregonstate.edu.
Centre National de la Recherche Scientifique · FROregon State University · USUniversité Paris-Sud · FR

Funding

Dynein light chain as a dimerization hub for natively disordered proteinsR01GM084276 · NIGMS · OREGON STATE UNIVERSITY · PI BARBAR, ELISAR J · 2009 to 2013
$1.5M
Acquisition of a 700 MHz NMR SpectrometerS10OD018518 · OD · OREGON STATE UNIVERSITY · PI BARBAR, ELISAR J · 2015 to 2015
$1.3M
NIGMS NIH HHS R01 GM084276NIH HHS S10 OD018518
6 · The paper itself

Abstract

The rabies and Ebola viruses recruit the highly conserved host protein LC8 for their own reproductive success. In vivo knockouts of the LC8 recognition motif within the rabies virus phosphoprotein (RavP) result in completely nonlethal viral infections. In this work, we examine the molecular role LC8 plays in viral lethality. We show that RavP and LC8 colocalize in rabies infected cells, and that LC8 interactions are essential for efficient viral polymerase functionality. NMR, SAXS, and molecular modeling demonstrate that LC8 binding to a disordered linker adjacent to an endogenous dimerization domain results in restrictions in RavP domain orientations. The resulting ensemble structure of RavP-LC8 tetrameric complex is similar to that of a related virus phosphoprotein that does not bind LC8, suggesting that with RavP, LC8 binding acts as a switch to induce a more active conformation. The high conservation of the LC8 motif in Lyssavirus phosphoproteins and its presence in other analogous proteins such as the Ebola virus VP35 evinces a broader purpose for LC8 in regulating downstream phosphoprotein functions vital for viral replication.

Indexed as

Conserved SequenceDNA-Directed RNA PolymerasesDrosophila ProteinsDyneinsEnzyme ActivationHost-Pathogen InteractionsLyssavirusModels, BiologicalModels, MolecularMultiprotein ComplexesPhosphoproteinsProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationRabies virusctp protein, DrosophilaDNA-Directed RNA PolymerasesDrosophila ProteinsDyneinsMultiprotein ComplexesPhosphoproteinsSTAT1 Transcription FactorViral ProteinsIntrinsically disordered proteinsNMRProtein interactionsSAXSVirus

Identifiers

PMID31634467
PMCPMC7060403
OpenAlexW2981312234

What OpenQuestion holds

Textmetadata
LicenceTDM
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.