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A common viral target is the alpha subunit of eukaryotic initiation factor 2 (eIF2\u03b1). In this study, we show that global protein synthesis was increased but the eIF2\u03b1 phosphorylation level was markedly decreased in porcine kidney 15 (PK15) cells infected with pseudorabies virus (PRV), a swine herpesvirus. An increase in the eIF2\u03b1 phosphorylation level by salubrinal treatment or transfection of constructs expressing wild-type eIF2\u03b1 or an eIF2\u03b1 phosphomimetic [eIF2\u03b1(S51D)] attenuated global protein synthesis and suppressed PRV replication. To explore the mechanism involved in the inhibition of eIF2\u03b1 phosphorylation during PRV infection, we examined the phosphorylation status of protein kinase R-like endoplasmic reticulum kinase (PERK) and double-stranded RNA-dependent protein kinase R (PKR), two kinases that regulate eIF2\u03b1 phosphorylation during infection with numerous viruses. We found that the level of neither phosphorylated (p)-PERK nor p-PKR was altered in PRV-infected cells or the lungs of infected mice. However, the expression of growth arrest and DNA damage-inducible protein 34 (GADD34), which promotes eIF2\u03b1 dephosphorylation by recruiting protein phosphatase 1 (PP1), was significantly induced both in vivo and in vitro. Knockdown of GADD34 and inhibition of PP1 activity by okadaic acid treatment led to increased eIF2\u03b1 phosphorylation but significantly suppressed global protein synthesis and inhibited PRV replication. Collectively, these results demonstrated that PRV induces GADD34 expression to promote eIF2\u03b1 dephosphorylation, thereby maintaining de novo protein synthesis and facilitating viral replication.<\/jats:p>","DOI":"10.1186\/s13567-021-01018-5","type":"journal-article","created":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T16:03:53Z","timestamp":1640016233000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["GADD34-mediated dephosphorylation of eIF2\u03b1 facilitates pseudorabies virus replication by maintaining de novo protein synthesis"],"prefix":"10.1186","volume":"52","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7176-4089","authenticated-orcid":false,"given":"Ting","family":"Zhu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xueli","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hangkuo","family":"Xin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaohui","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaonuan","family":"Xue","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ji-Long","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Baomin","family":"Qi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2021,12,20]]},"reference":[{"key":"1018_CR1","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1099\/jgv.0.000426","volume":"97","author":"Y Liao","year":"2016","unstructured":"Liao Y, Gu F, Mao X, Niu Q, Wang H, Sun Y, Song C, Qiu X, Tan L, Ding C (2016) Regulation of de novo translation of host cells by manipulation of PERK\/PKR and GADD34-PP1 activity during Newcastle disease virus infection. 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