Evidence map›Paper›PMID 27587337›Full record

ArticleNature communications2016

Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins.

Chen Zhao, Haripriya Sridharan, Ran Chen, Darren P Baker, Shanshan Wang, Robert M Krug

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

77 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Mitochondrial checkpoint for interferon responses in macrophages.Exploration of targeted anti-tumor therapy · 2026
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. ISG-15, beyond its functions in the cell: a mini review.Cellular and molecular life sciences : CMLS · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

17 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

6 authors at 2 institutions in 1 country.

Chen ZhaoDepartment of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
Haripriya SridharanDepartment of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
Ran ChenDepartment of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
Darren P BakerBiogen, Inc., Cambridge, Massachusetts 02142, USA.
Shanshan WangDepartment of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
Robert M KrugDepartment of Molecular Biosciences, Center for Infectious Disease, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
The University of Texas at Austin · USBiogen (United States) · US

Funding

REPLICATION OF INFLUENZA VIRUSR01AI011772 · NIAID · UNIVERSITY OF TEXAS AUSTIN · PI KRUG, ROBERT M · 1985 to 2017
$10.7M
NIAID NIH HHS R01 AI011772
6 · The paper itself

Abstract

The ubiquitin-like protein ISG15 and its conjugation to proteins (ISGylation) are strongly induced by type I interferon. Influenza B virus encodes non-structural protein 1 (NS1B) that binds human ISG15 and provides an appropriate model for determining how ISGylation affects virus replication in human cells. Here using a recombinant virus encoding a NS1B protein defective in ISG15 binding, we show that NS1B counteracts ISGylation-mediated antiviral activity by binding and sequestering ISGylated viral proteins, primarily ISGylated viral nucleoprotein (NP), in infected cells. ISGylated NP that is not sequestered by mutant NS1B acts as a dominant-negative inhibitor of oligomerization of the more abundant unconjugated NP. Consequently formation of viral ribonucleoproteins that catalyse viral RNA synthesis is inhibited, causing decreased viral protein synthesis and virus replication. We verify that ISGylated NP is largely responsible for inhibition of viral RNA synthesis by generating recombinant viruses that lack known ISGylation sites in NP.

Indexed as

A549 CellsAnimalsCell LineChick EmbryoCytokinesDogsEndopeptidasesHumansInfluenza B virusMadin Darby Canine Kidney CellsProtein BindingRibonucleoproteinsRNA InterferenceRNA, Small InterferingRNA, ViralUbiquitinsCytokinesEndopeptidasesINS1 protein, influenza virusISG15 protein, humanRibonucleoproteinsRNA, Small InterferingRNA, ViralUbiquitinsUbiquitin ThiolesteraseUSP18 protein, humanViral Nonstructural Proteins

Identifiers

PMID27587337
PMCPMC5025834
OpenAlexW2516470062

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.