Evidence map›Paper›PMID 32467327›Full record

ArticleJournal of cell science2020

Proteomic and mechanistic dissection of the poxvirus-customized ribosome.

Stephen DiGiuseppe, Madeline G Rollins, Helen Astar, Natalia Khalatyan, Jeffrey N Savas, Derek Walsh

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Impacts of ribosomal RNA sequence variation on gene expression and phenotype.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  4. Article
  5. Specialized Ribosomes in Health and Disease.International journal of molecular sciences · 2023
    Review
  6. Ribosomes in poxvirus infection.Current opinion in virology · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Ribosomal control in RNA virus-infected cells.Frontiers in microbiology · 2022
    Review
  11. 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

6 authors at 1 institution in 1 country.

Stephen DiGiuseppeDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Madeline G RollinsDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Helen AstarDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Natalia KhalatyanDepartment of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Jeffrey N SavasDepartment of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Derek WalshDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA derek.walsh@northwestern.edu.ORCID 0000-0002-8756-4655
Northwestern University · US

Funding

Poxvirus manipulation of the host cell protein synthesis machineryR01AI127456 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Peter Shen, Derek Walsh · 2017 to 2026
$4.4M
Uncovering the mechanism of how poxviruses hijack the host translational machinery to promote infectionF32AI140566 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DIGIUSEPPE, STEPHEN A · 2018 to 2019
$112k
NIAID NIH HHS F32 AI140566NIAID NIH HHS R01 AI127456
6 · The paper itself

Abstract

Ribosomes are often viewed as protein synthesis machines that lack intrinsic regulatory capacity. However, studies have established that ribosomes can functionally diversify through changes in the composition of, or post-translational modifications to ribosomal subunit proteins (RPs). We recently found that poxviruses phosphorylate unique sites in the RP, receptor for activated C kinase 1 (RACK1) to enhance viral protein synthesis. Here, we developed approaches for large-scale proteomic analysis of ribosomes isolated from cells infected with different viruses. Beyond RACK1, we identified additional phosphorylation events within RPS2 and RPS28 that arise during poxvirus infection, but not other viruses tested. The modified sites lie within unstructured loop domains that position around the mRNA entry and exit channel, respectively, and site-substitution mutants revealed that each modified residue contributed differently to poxvirus replication. Our findings reveal the broader extent to which poxviruses customize host ribosomes and provide new insights into how ribosomes can functionally diversify.

Indexed as

PoxviridaeProteomicsDissectionProtein BiosynthesisRibosomal ProteinsRibosomesRibosomal ProteinsPhosphorylationPost-translational modificationPoxvirusRibosomeRPS

Identifiers

PMID32467327
PMCPMC7358139
OpenAlexW3030021580

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.