During viral infection, the host cell synthesizes high amounts of viral proteins, which often causes stress to the endoplasmic reticulum (eR). to manage abnormal eR stress, mammalian cells trigger a response called the unfolded protein response (UpR). previous studies have indicated that porcine reproductive and respiratory syndrome virus (pRRSV), an Arterivirus that has been devastating the swine industry worldwide, can induce eR stress and activate UpR, however, the activation pathways and the biological significance requires further investigation. In this study, we demonstrated that, among the three types of UPR pathways, PRRSV infection induced PERK and IRE1 pathways, but not the ATF6 pathway. Furthermore, the induction of UPR promoted PRRSV replication. We also found that pRRSV-induced UpR, particularly the peRK pathway, was involved in the induction of autophagy, a cellular degradation process that can alleviate cell stress. Besides, we also provided insights into the eR stress-mediated apoptosis in response to pRRSV infection. pRRSV infection induced the expression of the transcription factor CHOP, which activated caspase 3 and PARP led to ER stressmediated apoptosis. Using 3-Methyladenine (3-MA) to inhibit autophagy, the increased ER stress and cell apoptosis were observed in the pRRSV infected cell. taken together, our results revealed the associations of eR stress, autophagy, and apoptosis during pRRSV infection, helping us to further understand how pRRSV interacts with host cells. Porcine reproductive and respiratory syndrome (PRRS) caused by PRRS virus (PRRSV), is one of the most economically significant disease in the swine industry 1. PRRSV belongs to the Nidovirales order, Arteriviridae family of positive-sense single-stranded RNA viruses 2. The burden of PRRSV infection on the host cell has been shown to initiate a number of cellular stress responses. Here, we focused on the endoplasmic reticulum (ER) stress during PRRSV infection. The ER is an extensive membranous network that provides a unique environment for the synthesis, maturation, and proper folding of a wide range of proteins. It also plays a critical role in the regulation of calcium concentration and intracellular signal transduction. Endogenous imbalances in cells, such as the accumulation of misfolded or unfolded proteins, can cause a stress to the ER system. To alleviate this stress, the unfolded protein response (UPR) is activated. The UPR eliminates misfolded or unfolded proteins in different ways: (1)
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