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. 2021 May 25;7:38. doi: 10.1038/s41421-021-00275-0

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — After coronavirus infection, the viral dsRNA binds to PKR, facilitating dimerization/oligomerization and autophosphorylation of PKR. The activated PKR catalyzes the phosphorylation of eIF2α, leading to the recruitment of SG-nucleating proteins, such as TIA-1 and G3BP1, and eventually SGs assembly. The NPs of SARS-CoV-2, SARS-CoV, and MERS-CoV can inhibit PKR phosphorylation, leading to the impairment of SG formation. The NPs of SARS-CoV-2 and SARS-CoV, but not MERS-CoV can also sequester G3BP1 to impair G3BP1-mediated SG assembly.