Evidence map›Paper›PMID 34696459›Full record

ArticleViruses2021

USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination.

Yingchong Wang, Qin Li, Dingwen Hu, Daolong Gao, Wenbiao Wang, Kailang Wu, Jianguo Wu

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Envelope Protein-Targeting Zika Virus Entry Inhibitors.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Ubiquitin-specific protease 38 promotes inflammatory atrial fibrillation induced by pressure overload.Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology · 2023
    Article
  17. Article
  18. Pathogenesis of Zika Virus Infection.Annual review of pathology · 2023
    Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Yingchong WangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Qin LiState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Dingwen HuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Daolong GaoGuangdong Longfan Biological Science and Technology Company, Shunde District, Foshan 528315, China.
Wenbiao WangGuangdong Provincial Key Laboratory of Virology, Institute of Medical Microbiology, Jinan University, Guangzhou 510632, China.
Kailang WuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
Jianguo WuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.ORCID 0000-0002-8326-2895
Wuhan University · CNJinan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zika virus (ZIKV) is a mosquito-borne flavivirus, and its infection may cause severe neurodegenerative diseases. The outbreak of ZIKV in 2015 in South America has caused severe human congenital and neurologic disorders. Thus, it is vitally important to determine the inner mechanism of ZIKV infection. Here, our data suggested that the ubiquitin-specific peptidase 38 (USP38) played an important role in host resistance to ZIKV infection, during which ZIKV infection did not affect USP38 expression. Mechanistically, USP38 bound to the ZIKV envelope (E) protein through its C-terminal domain and attenuated its K48-linked and K63-linked polyubiquitination, thereby repressed the infection of ZIKV. In addition, we found that the deubiquitinase activity of USP38 was essential to inhibit ZIKV infection, and the mutant that lacked the deubiquitinase activity of USP38 lost the ability to inhibit infection. In conclusion, we found a novel host protein USP38 against ZIKV infection, and this may represent a potential therapeutic target for the treatment and prevention of ZIKV infection.

Indexed as

UbiquitinationA549 CellsHeLa CellsHumansReceptor, EphB2Ubiquitin-Specific ProteasesViral Envelope ProteinsZika VirusZika Virus InfectionEPHB2 protein, humanReceptor, EphB2Ubiquitin-Specific ProteasesUSP38 protein, humanViral Envelope Proteinsdeubiquitinaseenvelope proteinUSP38virus infectionZika virus

Identifiers

PMID34696459
PMCPMC8538320
OpenAlexW3207091078

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.