The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins
Host–virus protein interactions are critical for intracellular viral propagation. Understanding the interactions between cellular and viral proteins may help us develop new antiviral strategies. Porcine epidemic diarrhea virus (PEDV) is a highly contagious coronavirus that causes severe damage to th...
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2022-10-01
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Online Access: | https://www.mdpi.com/1999-4915/14/10/2269 |
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author | Jianwei Zhou Yonghui Qiu Jie Zhao Yongxia Wang Ning Zhu Dedong Wang Yongqiu Cui Jinshuo Guo Tong Sun Ying Ji Zhi Wu Penghui Zeng Jingyi Li Xufei Feng Lei Hou Jue Liu |
author_facet | Jianwei Zhou Yonghui Qiu Jie Zhao Yongxia Wang Ning Zhu Dedong Wang Yongqiu Cui Jinshuo Guo Tong Sun Ying Ji Zhi Wu Penghui Zeng Jingyi Li Xufei Feng Lei Hou Jue Liu |
author_sort | Jianwei Zhou |
collection | DOAJ |
description | Host–virus protein interactions are critical for intracellular viral propagation. Understanding the interactions between cellular and viral proteins may help us develop new antiviral strategies. Porcine epidemic diarrhea virus (PEDV) is a highly contagious coronavirus that causes severe damage to the global swine industry. Here, we employed co-immunoprecipitation and liquid chromatography-mass spectrometry to characterize 426 unique PEDV nucleocapsid (N) protein-binding proteins in infected Vero cells. A protein–protein interaction network (PPI) was created, and gene ontology (GO) annotation and Kyoto Encyclopedia of Genes and Genomes (KEGG) database analyses revealed that the PEDV N-bound proteins belong to different cellular pathways, such as nucleic acid binding, ribonucleoprotein complex binding, RNA methyltransferase, and polymerase activities. Interactions of the PEDV N protein with 11 putative proteins: tripartite motif containing 21, DEAD-box RNA helicase 24, G3BP stress granule assembly factor 1, heat shock protein family A member 8, heat shock protein 90 alpha family class B member 1, YTH domain containing 1, nucleolin, Y-box binding protein 1, vimentin, heterogeneous nuclear ribonucleoprotein A2/B1, and karyopherin subunit alpha 1, were further confirmed by in vitro co-immunoprecipitation assay. In summary, studying an interaction network can facilitate the identification of antiviral therapeutic strategies and novel targets for PEDV infection. |
first_indexed | 2024-03-09T19:23:30Z |
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id | doaj.art-f9d074b01c4a4ed688a0ce5db28f5a50 |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-09T19:23:30Z |
publishDate | 2022-10-01 |
publisher | MDPI AG |
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series | Viruses |
spelling | doaj.art-f9d074b01c4a4ed688a0ce5db28f5a502023-11-24T03:10:34ZengMDPI AGViruses1999-49152022-10-011410226910.3390/v14102269The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular ProteinsJianwei Zhou0Yonghui Qiu1Jie Zhao2Yongxia Wang3Ning Zhu4Dedong Wang5Yongqiu Cui6Jinshuo Guo7Tong Sun8Ying Ji9Zhi Wu10Penghui Zeng11Jingyi Li12Xufei Feng13Lei Hou14Jue Liu15College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Animal Science and Technology, Anhui Agricultural University, Hefei 230036, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaCollege of Veterinary Medicine, Yangzhou University, Yangzhou 225009, ChinaHost–virus protein interactions are critical for intracellular viral propagation. Understanding the interactions between cellular and viral proteins may help us develop new antiviral strategies. Porcine epidemic diarrhea virus (PEDV) is a highly contagious coronavirus that causes severe damage to the global swine industry. Here, we employed co-immunoprecipitation and liquid chromatography-mass spectrometry to characterize 426 unique PEDV nucleocapsid (N) protein-binding proteins in infected Vero cells. A protein–protein interaction network (PPI) was created, and gene ontology (GO) annotation and Kyoto Encyclopedia of Genes and Genomes (KEGG) database analyses revealed that the PEDV N-bound proteins belong to different cellular pathways, such as nucleic acid binding, ribonucleoprotein complex binding, RNA methyltransferase, and polymerase activities. Interactions of the PEDV N protein with 11 putative proteins: tripartite motif containing 21, DEAD-box RNA helicase 24, G3BP stress granule assembly factor 1, heat shock protein family A member 8, heat shock protein 90 alpha family class B member 1, YTH domain containing 1, nucleolin, Y-box binding protein 1, vimentin, heterogeneous nuclear ribonucleoprotein A2/B1, and karyopherin subunit alpha 1, were further confirmed by in vitro co-immunoprecipitation assay. In summary, studying an interaction network can facilitate the identification of antiviral therapeutic strategies and novel targets for PEDV infection.https://www.mdpi.com/1999-4915/14/10/2269porcine epidemic diarrhea virusnucleocapsid proteininteraction networkGO analysisKEGG analysis |
spellingShingle | Jianwei Zhou Yonghui Qiu Jie Zhao Yongxia Wang Ning Zhu Dedong Wang Yongqiu Cui Jinshuo Guo Tong Sun Ying Ji Zhi Wu Penghui Zeng Jingyi Li Xufei Feng Lei Hou Jue Liu The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins Viruses porcine epidemic diarrhea virus nucleocapsid protein interaction network GO analysis KEGG analysis |
title | The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins |
title_full | The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins |
title_fullStr | The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins |
title_full_unstemmed | The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins |
title_short | The Network of Interactions between the Porcine Epidemic Diarrhea Virus Nucleocapsid and Host Cellular Proteins |
title_sort | network of interactions between the porcine epidemic diarrhea virus nucleocapsid and host cellular proteins |
topic | porcine epidemic diarrhea virus nucleocapsid protein interaction network GO analysis KEGG analysis |
url | https://www.mdpi.com/1999-4915/14/10/2269 |
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