Evidence map›Paper›PMID 20660183›Full record

ArticleJournal of virology2010

An interaction between the nucleocapsid protein and a component of the replicase-transcriptase complex is crucial for the infectivity of coronavirus genomic RNA.

Kelley R Hurst, Rong Ye, Scott J Goebel, Priya Jayaraman, Paul S Masters

Abstract 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 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
–field-weighted citation impact
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

93 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Caution urged for work with newly constructed human coronavirus.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Nsp3-N interactions are critical for SARS-CoV-2 fitness and virulence.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

33 more citing papers are in PubMed but not listed here.

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

5 authors.

Kelley R HurstWadsworth Center, New York State Department of Health, Albany, NY 12201, USA.
Rong Ye
Scott J Goebel
Priya Jayaraman
Paul S Masters

Funding

Genetic Analysis of Molecular Interactions in Coronavirus ReplicationR01AI064603 · NIAID · WADSWORTH CENTER · PI MASTERS, PAUL SCOTT · 2005 to 2015
$4.7M
Genetic Analysis of Molecular Interactions in Coronavirus ReplicationR56AI064603 · NIAID · WADSWORTH CENTER · PI MASTERS, PAUL SCOTT · 2010 to 2010
$536k
NIAID NIH HHS AI 64603NIAID NIH HHS R01 AI064603NIAID NIH HHS R56 AI064603
6 · The paper itself

Abstract

The coronavirus nucleocapsid (N) protein plays an essential role in virion assembly via interactions with the large, positive-strand RNA viral genome and the carboxy-terminal endodomain of the membrane protein (M). To learn about the functions of N protein domains in the coronavirus mouse hepatitis virus (MHV), we replaced the MHV N gene with its counterpart from the closely related bovine coronavirus (BCoV). The resulting viral mutant was severely defective, even though individual domains of the N protein responsible for N-RNA, N-M, or N-N interactions were completely interchangeable between BCoV and MHV. The lesion in the BCoV N substitution mutant could be compensated for by reverting mutations in the central, serine- and arginine-rich (SR) domain of the N protein. Surprisingly, a second class of reverting mutations were mapped to the amino terminus of a replicase subunit, nonstructural protein 3 (nsp3). A similarly defective MHV N mutant bearing an insertion of the SR region from the severe acute respiratory syndrome coronavirus N protein was rescued by the same two classes of reverting mutations. Our genetic results were corroborated by the demonstration that the expressed amino-terminal segment of nsp3 bound selectively to N protein from infected cells, and this interaction was RNA independent. Moreover, we found a direct correlation between the N-nsp3 interaction and the ability of N protein to stimulate the infectivity of transfected MHV genomic RNA (gRNA). Our results suggest a role for this previously unknown N-nsp3 interaction in the localization of genomic RNA to the replicase complex at an early stage of infection.

Indexed as

Amino Acid SequenceAnimalsCattleCoronavirus, BovineCoronavirus Nucleocapsid ProteinsDNA-Directed RNA PolymerasesGenome, ViralHumansMiceMolecular Sequence DataMurine hepatitis virusMutationNucleocapsid ProteinsProtein Structure, TertiaryRecombination, GeneticRNA-Dependent RNA PolymeraseCoronavirus Nucleocapsid ProteinsDNA-Directed RNA PolymerasesNucleocapsid ProteinsRNA-Dependent RNA PolymeraseRNA, Viral

Identifiers

PMID20660183
PMCPMC2937748

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.