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The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε
Porcine reproductive and respiratory syndrome (PRRS) caused by PRRS virus (PRRSV) is one of the most severe swine diseases that affects almost all swine-breeding countries. Nonstructural protein 2 (NSP2) is one of the most important viral proteins in the PRRSV life cycle. Our previous study showed t...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7433210/ https://www.ncbi.nlm.nih.gov/pubmed/32811532 http://dx.doi.org/10.1186/s13567-020-00816-7 |
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author | Cao, Shengliang Liu, Jiaqi Ding, Guofei Shao, Qingyuan Wang, Bin Li, Yingchao Feng, Jian Zhao, Yuzhong Liu, Sidang Xiao, Yihong |
author_facet | Cao, Shengliang Liu, Jiaqi Ding, Guofei Shao, Qingyuan Wang, Bin Li, Yingchao Feng, Jian Zhao, Yuzhong Liu, Sidang Xiao, Yihong |
author_sort | Cao, Shengliang |
collection | PubMed |
description | Porcine reproductive and respiratory syndrome (PRRS) caused by PRRS virus (PRRSV) is one of the most severe swine diseases that affects almost all swine-breeding countries. Nonstructural protein 2 (NSP2) is one of the most important viral proteins in the PRRSV life cycle. Our previous study showed that PRRSV NSP2 could induce the formation of aggresomes. In this study we explored the effects of aggresome formation on cells and found that NSP2 could induce autophagy, which depended on aggresome formation to activate aggrephagy. The transmembrane and tail domains of NSP2 contributed to aggrephagy and the cellular protein 14-3-3ε played an important role in NSP2-induced autophagy by binding the tail domain of NSP2. These findings provide information on the function of the C-terminal domain of NSP2, which will help uncover the function of NSP2 during PRRSV infection. |
format | Online Article Text |
id | pubmed-7433210 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-74332102020-08-19 The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε Cao, Shengliang Liu, Jiaqi Ding, Guofei Shao, Qingyuan Wang, Bin Li, Yingchao Feng, Jian Zhao, Yuzhong Liu, Sidang Xiao, Yihong Vet Res Research Article Porcine reproductive and respiratory syndrome (PRRS) caused by PRRS virus (PRRSV) is one of the most severe swine diseases that affects almost all swine-breeding countries. Nonstructural protein 2 (NSP2) is one of the most important viral proteins in the PRRSV life cycle. Our previous study showed that PRRSV NSP2 could induce the formation of aggresomes. In this study we explored the effects of aggresome formation on cells and found that NSP2 could induce autophagy, which depended on aggresome formation to activate aggrephagy. The transmembrane and tail domains of NSP2 contributed to aggrephagy and the cellular protein 14-3-3ε played an important role in NSP2-induced autophagy by binding the tail domain of NSP2. These findings provide information on the function of the C-terminal domain of NSP2, which will help uncover the function of NSP2 during PRRSV infection. BioMed Central 2020-08-18 2020 /pmc/articles/PMC7433210/ /pubmed/32811532 http://dx.doi.org/10.1186/s13567-020-00816-7 Text en © The Author(s) 2020 Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Article Cao, Shengliang Liu, Jiaqi Ding, Guofei Shao, Qingyuan Wang, Bin Li, Yingchao Feng, Jian Zhao, Yuzhong Liu, Sidang Xiao, Yihong The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title | The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title_full | The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title_fullStr | The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title_full_unstemmed | The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title_short | The tail domain of PRRSV NSP2 plays a key role in aggrephagy by interacting with 14-3-3ε |
title_sort | tail domain of prrsv nsp2 plays a key role in aggrephagy by interacting with 14-3-3ε |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7433210/ https://www.ncbi.nlm.nih.gov/pubmed/32811532 http://dx.doi.org/10.1186/s13567-020-00816-7 |
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