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Article: M1 of murine gamma-herpesvirus 68 induces endoplasmic reticulum chaperone production

TitleM1 of murine gamma-herpesvirus 68 induces endoplasmic reticulum chaperone production
Authors
Issue Date2015
Citation
Scientific Reports, 2015, v. 5, article no. 17228 How to Cite?
AbstractViruses rely on host chaperone network to support their infection. In particular, the endoplasmic reticulum (ER) resident chaperones play key roles in synthesizing and processing viral proteins. Influx of a large amount of foreign proteins exhausts the folding capacity in ER and triggers the unfolded protein response (UPR). A fully-executed UPR comprises signaling pathways that induce ER folding chaperones, increase protein degradation, block new protein synthesis and may eventually activate apoptosis, presenting both opportunities and threats to the virus. Here, we define a role of the MHV-68M1 gene in differential modulation of UPR pathways to enhance ER chaperone production. Ectopic expression of M1 markedly induces ER chaperone genes and expansion of ER. The M1 protein accumulates in ER during infection and this localization is indispensable for its function, suggesting M1 acts from the ER. We found that M1 protein selectively induces the chaperon-producing pathways (IRE1, ATF6) while, interestingly, sparing the translation-blocking arm (PERK). We identified, for the first time, a viral factor capable of selectively intervening the initiation of ER stress signaling to induce chaperon production. This finding provides a unique opportunity of using viral protein as a tool to define the activation mechanisms of individual UPR pathways.
Persistent Identifierhttp://hdl.handle.net/10722/285887
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorFeng, Jiaying-
dc.contributor.authorGong, Danyang-
dc.contributor.authorFu, Xudong-
dc.contributor.authorWu, Ting Ting-
dc.contributor.authorWang, Jane-
dc.contributor.authorChang, Jennifer-
dc.contributor.authorZhou, Jingting-
dc.contributor.authorLu, Gang-
dc.contributor.authorWang, Yibin-
dc.contributor.authorSun, Ren-
dc.date.accessioned2020-08-18T04:56:54Z-
dc.date.available2020-08-18T04:56:54Z-
dc.date.issued2015-
dc.identifier.citationScientific Reports, 2015, v. 5, article no. 17228-
dc.identifier.urihttp://hdl.handle.net/10722/285887-
dc.description.abstractViruses rely on host chaperone network to support their infection. In particular, the endoplasmic reticulum (ER) resident chaperones play key roles in synthesizing and processing viral proteins. Influx of a large amount of foreign proteins exhausts the folding capacity in ER and triggers the unfolded protein response (UPR). A fully-executed UPR comprises signaling pathways that induce ER folding chaperones, increase protein degradation, block new protein synthesis and may eventually activate apoptosis, presenting both opportunities and threats to the virus. Here, we define a role of the MHV-68M1 gene in differential modulation of UPR pathways to enhance ER chaperone production. Ectopic expression of M1 markedly induces ER chaperone genes and expansion of ER. The M1 protein accumulates in ER during infection and this localization is indispensable for its function, suggesting M1 acts from the ER. We found that M1 protein selectively induces the chaperon-producing pathways (IRE1, ATF6) while, interestingly, sparing the translation-blocking arm (PERK). We identified, for the first time, a viral factor capable of selectively intervening the initiation of ER stress signaling to induce chaperon production. This finding provides a unique opportunity of using viral protein as a tool to define the activation mechanisms of individual UPR pathways.-
dc.languageeng-
dc.relation.ispartofScientific Reports-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleM1 of murine gamma-herpesvirus 68 induces endoplasmic reticulum chaperone production-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/srep17228-
dc.identifier.pmid26615759-
dc.identifier.pmcidPMC4663489-
dc.identifier.scopuseid_2-s2.0-84948697003-
dc.identifier.volume5-
dc.identifier.spagearticle no. 17228-
dc.identifier.epagearticle no. 17228-
dc.identifier.eissn2045-2322-

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