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

Xiaozhen Guo; Kejian Yu; Zhonghao Xin; Liping Liu; Yuehua Gao; Feng Hu; Xiuli Ma; Kexiang Yu; Yufeng Li; Bing Huang; Zhengui Yan; Jiaqiang Wu

doi:10.3389/fmicb.2022.931922

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

Front Microbiol. 2022 Jul 4:13:931922. doi: 10.3389/fmicb.2022.931922. eCollection 2022.

Authors

Xiaozhen Guo¹, Kejian Yu², Zhonghao Xin², Liping Liu¹, Yuehua Gao¹, Feng Hu¹, Xiuli Ma¹, Kexiang Yu¹, Yufeng Li¹, Bing Huang¹, Zhengui Yan², Jiaqiang Wu^{2

3

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Affiliations

¹ Shandong Key Laboratory of Immunity and Diagnosis of Poultry Diseases, Institute of Poultry Science, Shandong Academy of Agricultural Sciences, Jinan, China.
² Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, College of Animal Science and Technology, Shandong Agricultural University, Taian, China.
³ Shandong Key Laboratory of Disease Control and Breeding, Institute of Animal Science and Veterinary Medicine, Shandong Academy of Agricultural Science, Jinan, China.
⁴ Shandong Key Laboratory of Animal Resistant Biology, College of Life Sciences, Shandong Normal University, Jinan, China.

Abstract

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.

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