Evidence map›Paper›PMID 35435699›Full record

ArticlemBio2022

A Poxvirus Decapping Enzyme Colocalizes with Mitochondria To Regulate RNA Metabolism and Translation and Promote Viral Replication.

Shuai Cao, Joshua A Molina, Fernando Cantu, Candy Hernandez, Zhilong Yang

Open access · goldAbstract read
In one paragraph

Article in mBio, 2022. 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
2.5field-weighted citation impact, top 11% 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, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Ribosomes in poxvirus infection.Current opinion in virology · 2022
    Review
  10. Article
  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

5 authors at 2 institutions in 1 country.

Shuai CaoDepartment of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas, USA.
Joshua A MolinaDepartment of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas, USA.
Fernando CantuDivision of Biology, Kansas State Universitygrid.36567.31, Manhattan, Kansas, USA.ORCID 0000-0002-2794-8761
Candy HernandezDepartment of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas, USA.
Zhilong YangDepartment of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, Texas, USA.ORCID 0000-0001-8995-2654
Kansas State University · USTexas A&M University · US

Funding

Mechanisms regulating poxvirus post-replicative protein synthesisR01AI143709 · NIAID · TEXAS A&M AGRILIFE RESEARCH · PI YANG, ZHILONG · 2019 to 2023
$1.9M
NIAID NIH HHS R01 AI143709
6 · The paper itself

Abstract

Decapping enzymes remove the 5' cap of eukaryotic mRNA, leading to accelerated RNA decay. They are critical in regulating RNA homeostasis and play essential roles in many cellular and life processes. They are encoded in many organisms and viruses, including vaccinia virus, which was used as the vaccine to eradicate smallpox. Vaccinia virus encodes two decapping enzymes, D9 and D10, that are necessary for efficient viral replication and pathogenesis. However, the underlying molecular mechanisms regulating vaccinia decapping enzymes' functions are still largely elusive. Here, we demonstrated that vaccinia D10 almost exclusively colocalized with mitochondria. As mitochondria are highly mobile cellular organelles, colocalization of D10 with mitochondria can concentrate D10 locally and mobilize it to efficiently decap mRNAs. Mitochondria were barely observed in "viral factories," where viral transcripts are produced, suggesting that mitochondrial colocalization provides a spatial mechanism to preferentially decap cellular mRNAs over viral mRNAs. We identified three amino acids at the N terminus of D10 that are required for D10's mitochondrial colocalization. Loss of mitochondrial colocalization significantly impaired viral replication, reduced D10's ability to remove the RNA 5' cap during infection, and diminished D10's gene expression shutoff and mRNA translation promotion abilities.

Indexed as

VacciniaAnimalsEndoribonucleasesMitochondriaRNA CapsRNA, MessengerRNA, ViralVaccinia virusViral ProteinsVirus ReplicationEndoribonucleasesmRNA decapping enzymesRNA CapsRNA, MessengerRNA, ViralViral ProteinsD10decapping enzymemitochondriapoxvirusRNA decaytranslationtranslational controlvaccinia virus

Identifiers

PMID35435699
PMCPMC9239241
OpenAlexW4223977034

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.