Evidence map›Paper›PMID 32354743›Full record

ArticleThe Journal of biological chemistry2020

Guanylate-binding protein 2 orchestrates innate immune responses against murine norovirus and is antagonized by the viral protein NS7.

Peifa Yu, Yang Li, Yunlong Li, Zhijiang Miao, Maikel P Peppelenbosch, Qiuwei Pan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.7field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  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

6 authors at 1 institution in 1 country.

Peifa YuDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands p.yu@erasmusmc.nl q.pan@erasmusmc.nl.ORCID 0000-0003-2255-0508
Yang LiDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands.
Yunlong LiDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands.
Zhijiang MiaoDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands.
Maikel P PeppelenboschDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands.ORCID 0000-0001-9982-6184
Qiuwei PanDepartment of Gastroenterology and Hepatology, Erasmus MC-University Medical Center, Rotterdam, The Netherlands p.yu@erasmusmc.nl q.pan@erasmusmc.nl.
Erasmus MC · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Noroviruses are the main causative agents of acute viral gastroenteritis, but the host factors that restrict their replication remain poorly identified. Guanylate-binding proteins (GBPs) are interferon (IFN)-inducible GTPases that exert broad antiviral activity and are important mediators of host defenses against viral infections. Here, we show that both IFN-γ stimulation and murine norovirus (MNV) infection induce GBP2 expression in murine macrophages. Results from loss- and gain-of-function assays indicated that GBP2 is important for IFN-γ-dependent anti-MNV activity in murine macrophages. Ectopic expression of MNV receptor (CD300lf) in human HEK293T epithelial cells conferred susceptibility to MNV infection. Importantly, GBP2 potently inhibited MNV in these human epithelial cells. Results from mechanistic dissection experiments revealed that the N-terminal G domain of GBP2 mediates these anti-MNV effects. R48A and K51A substitutions in GBP2, associated with loss of GBP2 GTPase activity, attenuated the anti-MNV effects of GBP2. Finally, we found that nonstructural protein 7 (NS7) of MNV co-localizes with GBP2 and antagonizes the anti-MNV activity of GBP2. These findings reveal that GBP2 is an important mediator of host defenses against murine norovirus.

Indexed as

Immunity, InnateAnimalsChlorocebus aethiopsCOS CellsGTP-Binding ProteinsHEK293 CellsHumansInterferon-gammaMacrophagesMiceNorovirusRAW 264.7 CellsViral Nonstructural ProteinsGbp2 protein, mouseGTP-Binding ProteinsInterferon-gammaViral Nonstructural Proteinsantiviral restriction factorGTPaseguanylate-binding protein 2 (GBP2)host defensehost-pathogen interactioninnate immunityinterferon-stimulated gene (ISG)murine norovirus (MNV)non-structural protein 7 (NS7)viral replication

Identifiers

PMID32354743
PMCPMC7278355
OpenAlexW3022305939

What OpenQuestion holds

Textmetadata
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.