Evidence map›Paper›PMID 21047957›Full record

ArticleJournal of virology2011

Modification of nonstructural protein 1 of influenza A virus by SUMO1.

Ke Xu, Christoph Klenk, Bin Liu, Bjoern Keiner, Jinke Cheng, Bo-Jian Zheng, Li Li, Qinglin Han, Chen Wang, Tianxian Li and 5 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. SUMOylation in Viral Replication and Antiviral Defense.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. SUMO: a novel target for anti-coronavirus therapy.Pathogens and global health · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. SUMO and SUMOylation Pathway at the Forefront of Host Immune Response.Frontiers in cell and developmental biology · 2021
    Review

1 more citing papers are in PubMed but not listed here.

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

15 authors at 10 institutions in 3 countries.

Ke XuLaboratory of Molecular Virology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, 225 South Chongqing Road, Shanghai 200025, China.
Christoph Klenk
Bin Liu
Bjoern Keiner
Jinke Cheng
Bo-Jian Zheng
Li Li
Qinglin Han
Chen Wang
Tianxian Li
Ze Chen
Yuelong Shu
Jinhua Liu
Hans-Dieter Klenk
Bing Sun
Chinese Academy of Sciences · CNPhilipps University of Marburg · DEShanghai Jiao Tong University · CNCenter for Excellence in Molecular Cell Science · CNChina Agricultural University · CNChinese Center For Disease Control and Prevention · CNInstitut Pasteur of Shanghai · CNUniversity of Hong Kong · HKUniversity of Würzburg · DEWuhan Institute of Virology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonstructural protein 1 (NS1) is one of the major factors resulting in the efficient infection rate and high level of virulence of influenza A virus. Although consisting of only approximately 230 amino acids, NS1 has the ability to interfere with several systems of the host viral defense. In the present study, we demonstrate that NS1 of the highly pathogenic avian influenza A/Duck/Hubei/L-1/2004 (H5N1) virus interacts with human Ubc9, which is the E2 conjugating enzyme for sumoylation, and we show that SUMO1 is conjugated to H5N1 NS1 in both transfected and infected cells. Furthermore, two lysine residues in the C terminus of NS1 were identified as SUMO1 acceptor sites. When the SUMO1 acceptor sites were removed by mutation, NS1 underwent rapid degradation. Studies of different influenza A virus strains of human and avian origin showed that the majority of viruses possess an NS1 protein that is modified by SUMO1, except for the recently emerged swine-origin influenza A virus (S-OIV) (H1N1). Interestingly, growth of a sumoylation-deficient WSN virus mutant was retarded compared to that of wild-type virus. Together, these results indicate that sumoylation enhances NS1 stability and thus promotes rapid growth of influenza A virus.

Indexed as

Host-Pathogen InteractionsAnimalsCell LineDogsHumansImmunohistochemistryInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H5N1 SubtypeLysineMicroscopy, ConfocalMutagenesis, Site-DirectedProtein BindingSUMO-1 ProteinSumoylationTwo-Hybrid System TechniquesUbiquitin-Conjugating EnzymesINS1 protein, influenza virusLysineSUMO-1 ProteinSUMO1 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Viral Nonstructural Proteins

Identifiers

PMID21047957
PMCPMC3020006
OpenAlexW2169932752

What OpenQuestion holds

Textmetadata
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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.