Evidence map›Paper›PMID 28545059›Full record

ArticlePLoS pathogens2017

UGGT1 enhances enterovirus 71 pathogenicity by promoting viral RNA synthesis and viral replication.

Peng-Nien Huang, Jia-Rong Jheng, Jamie J Arnold, Jen-Ren Wang, Craig E Cameron, Shin-Ru Shih

Abstract read
In one paragraph

Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Spatial protein redistribution: wandering but not lost.Cellular and molecular life sciences : CMLS · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. A single mutation in theEmerging microbes & infections · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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.

Peng-Nien HuangResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
Jia-Rong JhengResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.ORCID http://orcid.org/0000-0002-9210-8611
Jamie J ArnoldDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, United States of America.ORCID http://orcid.org/0000-0002-2345-9776
Jen-Ren WangDepartment of Medical Laboratory Science and Biotechnology, National Cheng Kung University, Tainan, Taiwan.ORCID http://orcid.org/0000-0002-4127-4046
Craig E CameronDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, United States of America.
Shin-Ru ShihResearch Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.ORCID http://orcid.org/0000-0003-4874-401X

Funding

Picornavirus Genome ReplicationR37AI053531 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CRAIG E. CAMERON · 2018 to 2026
$4.8M
6 · The paper itself

Abstract

Positive-strand RNA virus infections can induce the stress-related unfolded protein response (UPR) in host cells. This study found that enterovirus A71 (EVA71) utilizes host UDP-glucose glycoprotein glucosyltransferase 1 (UGGT1), a key endoplasmic reticulum protein (ER) involved in UPR, to enhance viral replication and virulence. EVA71 forms replication complexes (RCs) on cellular membranes that contain a mix of host and viral proteins to facilitate viral replication, but the components and processes involved in the assembly and function of RCs are not fully understood. Using EVA71 as a model, this study found that host UGGT1 and viral 3D polymerase co-precipitate along with other factors on membranous replication complexes to enhance viral replication. Increased UGGT1 levels elevated viral growth rates, while viral pathogenicity was observed to be lower in heterozygous knockout mice (Uggt1 +/- mice). These findings provide important insight on the role of UPR and host UGGT1 in regulating RNA virus replication and pathogenicity.

Indexed as

Amino Acid SequenceAnimalsCell Line, TumorCell ProliferationCell SurvivalEndoplasmic ReticulumEnterovirus A, HumanGlucosyltransferasesHost-Pathogen InteractionsMiceMice, KnockoutRNA, ViralUDP-Galactose TranslocatorsUnfolded Protein ResponseViral ProteinsVirulenceGlucosyltransferasesRNA, ViralUDP-Galactose TranslocatorsUGGT1 protein, humanViral Proteins

Identifiers

PMID28545059
PMCPMC5435352

What OpenQuestion holds

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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.