About: Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis

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About: Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis
Creator	Wang, Dang Xiao, Shaobo Chen, Quangang Liu, Suyan Men, Yanjuan Xu, Deqin Liurong Fang, &
Source	Medline; PMC
abstract	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 stress-mediated 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.
has issue date	2020-08-04(xsd:dateTime)
bibo:doi	10.1038/s41598-020-69959-z
bibo:pmid	32753633
has license	cc-by
sha1sum (hex)	c2a2206ea78d84055927a72bf8c082d707cf0dc2
schema:url	https://doi.org/10.1038/s41598-020-69959-z
resource representing a document's title	Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis
has PubMed Central identifier	PMC7403369
has PubMed identifier	32753633
schema:publication	Sci Rep
resource representing a document's body	covid:c2a2206ea78d84055927a72bf8c082d707cf0dc2#body_text
is schema:about of	named entity 'response' named entity 'stress' named entity 'PERK' named entity 'insights' named entity 'autophagy' named entity 'induction' named entity 'endoplasmic reticulum' named entity 'reproductive' named entity 'apoptosis' named entity 'activated' named entity 'reproductive' named entity 'involved' named entity 'activate' named entity 'caspase' named entity 'revealed' named entity 'interacts' named entity 'ER stress' named entity 'IRE1' named entity 'virus' named entity 'caspase 3' named entity 'UpR' named entity '0.01' named entity 'signaling pathway' named entity 'antibodies' named entity 'mRNA' named entity 'stop codon' named entity 'ER stress' named entity 'infection' named entity 'infection' named entity 'Cell Signaling Technology' named entity 'RNAi' named entity 'ultrastructural' named entity 'RNA' named entity 'ER stress' named entity 'mRNA' named entity 'IRE1' named entity 'infection' named entity 'calreticulin' named entity 'viral proteins' named entity 'ATF6' named entity 'transcriptional' named entity 'PERK' named entity 'phosphorylation' named entity 'PERK' named entity 'molecular chaperone' named entity 'lysis buffer' named entity 'caspase 3' named entity 'African swine fever virus' named entity 'phosphorylation' named entity 'caspase 3' named entity 'ATF6' named entity 'infection' named entity 'signaling pathway' named entity 'mRNA splicing' named entity 'luciferase' named entity 'GFP' named entity 'UPR' named entity 'CHOP' named entity 'positive control' named entity 'virus' named entity 'reagent' named entity 'neutral red' named entity 'PERK' named entity 'apoptosis' named entity 'ATF6' named entity 'UPR' named entity 'China' named entity 'Renilla luciferase' named entity 'ATF6' named entity 'GRP94' named entity 'ER stress' named entity 'PERK' named entity 'UPR' named entity 'phosphorylated' named entity 'ATF6'

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