4.6 Article

Porcine Epidemic Diarrhea Virus Infection Subverts Arsenite-Induced Stress Granules Formation

Journal

FRONTIERS IN MICROBIOLOGY
Volume 13, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2022.931922

Keywords

PEDV replication; stress granules; sodium arsenite; papain-like protease; interaction mechanism

Categories

Funding

  1. Shandong Provincial Natural Science Foundation Youth Project [ZR2021QC054]
  2. Shandong Provincial Modern Agricultural Industry and Technology System [SDAIT-08-01]
  3. Great Scientific and Technological Innovation Projects in Shandong Province [2020CXGC010801]
  4. Shandong Key Provincial Research and Development Program [2019GNC106044]
  5. National Natural Science Funds [32070178, 32002286]
  6. Agricultural Scientific and Technological Innovation Project of Shandong Academy of Agricultural Sciences [CXGC2021A12, CXGC2021A39]

Ask authors/readers for more resources

This study found that PEDV-infected cells contain SGs and are resistant to SA-induced SGs formation. PEDV infection disrupts SGs formation by downregulating G3BP1 expression. PEDV replication is significantly enhanced when SGs assembly is impaired by silencing G3BP1.
Stress granules (SGs) are dynamic cytoplasmic protein-RNA structures that form in response to various stress conditions, including viral infection. Porcine epidemic diarrhea virus (PEDV) variant-related diarrhea has caused devastating economic losses to the swine industry worldwide. In this study, we found that the percentage of PEDV-infected cells containing SGs is nearly 20%; meanwhile, PEDV-infected cells were resistant to sodium arsenite (SA)-induced SGs formation, as demonstrated by the recruitment of SGs marker proteins, including G3BP1 and TIA1. Moreover, the formation of SGs induced by SA treatment was suppressed by PEDV papain-like protease confirmed by confocal microscopy. Further study showed that PEDV infection disrupted SGs formation by downregulating G3BP1 expression. Additionally, PEDV replication was significantly enhanced when SGs' assembly was impaired by silencing G3BP1. Taken together, our findings attempt to illuminate the specific interaction mechanism between SGs and PEDV, which will help us to elucidate the pathogenesis of PEDV infection in the near future.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available