Evidence map›Paper›PMID 39571001›Full record

ArticlePLoS pathogens2024

SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation.

Abdullah M Syed, Alison Ciling, Irene P Chen, Christopher R Carlson, Armin N Adly, Hannah S Martin, Taha Y Taha, Mir M Khalid, Nathan Price, Mehdi Bouhaddou and 6 more

Abstract read
In one paragraph

Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Article
  14. SARS-CoV-2 nucleocapsid protein directly prevents cGAS-DNA recognition through competitive binding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Assembly of SARS-CoV-2 ribonucleosomes by truncated NThe Journal of biological chemistry · 2023
    Article
  20. Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023
    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

16 authors.

Abdullah M SyedGladstone Institutes, San Francisco, California, United States of America.ORCID 0000-0001-9156-9662
Alison CilingGladstone Institutes, San Francisco, California, United States of America.
Irene P ChenGladstone Institutes, San Francisco, California, United States of America.
Christopher R CarlsonDepartment of Physiology, University of California, San Francisco, California, United States of America.
Armin N AdlyDepartment of Physiology, University of California, San Francisco, California, United States of America.
Hannah S MartinDepartment of Chemistry, University of California, Berkeley, California, United States of America.
Taha Y TahaGladstone Institutes, San Francisco, California, United States of America.
Mir M KhalidGladstone Institutes, San Francisco, California, United States of America.
Nathan PriceGladstone Institutes, San Francisco, California, United States of America.
Mehdi BouhaddouGladstone Institutes, San Francisco, California, United States of America.
Manisha R UmmadiGladstone Institutes, San Francisco, California, United States of America.
Jack M MoenGladstone Institutes, San Francisco, California, United States of America.
Nevan J KroganGladstone Institutes, San Francisco, California, United States of America.
David O MorganDepartment of Physiology, University of California, San Francisco, California, United States of America.
Melanie OttGladstone Institutes, San Francisco, California, United States of America.
Jennifer A DoudnaGladstone Institutes, San Francisco, California, United States of America.ORCID 0000-0001-9161-999X

Funding

SARS-CoV adaptations through a Systems Biology Lens (SYBIL)U19AI135972 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Adolfo Garcia-Sastre · 2018 to 2026
$27.2M
RESEARCH PROJECT 2U19AI135990 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Melanie Maria Ott · 2018 to 2026
$21.4M
Regulatory Enzymes and Systems in Cell Cycle ControlR35GM118053 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVID Owen MORGAN · 2016 to 2026
$10.3M
NIAID NIH HHS U19 AI135972NIAID NIH HHS U19 AI135990NIGMS NIH HHS R35 GM118053
6 · The paper itself

Abstract

All lineages of SARS-CoV-2, the coronavirus responsible for the COVID-19 pandemic, contain mutations between amino acids 199 and 205 in the nucleocapsid (N) protein that are associated with increased infectivity. The effects of these mutations have been difficult to determine because N protein contributes to both viral replication and viral particle assembly during infection. Here, we used single-cycle infection and virus-like particle assays to show that N protein phosphorylation has opposing effects on viral assembly and genome replication. Ancestral SARS-CoV-2 N protein is densely phosphorylated, leading to higher levels of genome replication but 10-fold lower particle assembly compared to evolved variants with low N protein phosphorylation, such as Delta (N:R203M), Iota (N:S202R), and B.1.2 (N:P199L). A new open reading frame encoding a truncated N protein called N*, which occurs in the B.1.1 lineage and subsequent lineages of the Alpha, Gamma, and Omicron variants, supports high levels of both assembly and replication. Our findings help explain the enhanced fitness of viral variants of concern and a potential avenue for continued viral selection.

Indexed as

Coronavirus Nucleocapsid ProteinsCOVID-19Evolution, MolecularPhosphoproteinsSARS-CoV-2Virus ReplicationAnimalsChlorocebus aethiopsHumansMutationPhosphorylationVero CellsVirus AssemblyCoronavirus Nucleocapsid Proteinsnucleocapsid phosphoprotein, SARS-CoV-2Phosphoproteins

Identifiers

PMID39571001
PMCPMC11620656

What OpenQuestion holds

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LicenceCC BY
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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.