The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein
Abstract The transport of circovirus capsid protein into nucleus is essential for viral replication in infected cell. However, the role of nucleolar shuttle proteins during porcine circovirus 3 capsid protein (PCV3 Cap) import is still not understood. Here, we report a previously unidentified nucleo...
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| Format: | Article |
| Language: | English |
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BMC
2021-01-01
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| Series: | Veterinary Research |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s13567-020-00876-9 |
| _version_ | 1818461600717209600 |
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| author | Jianwei Zhou Juan Li Haimin Li Ying Zhang Weiren Dong Yulan Jin Yan Yan Jinyan Gu Jiyong Zhou |
| author_facet | Jianwei Zhou Juan Li Haimin Li Ying Zhang Weiren Dong Yulan Jin Yan Yan Jinyan Gu Jiyong Zhou |
| author_sort | Jianwei Zhou |
| collection | DOAJ |
| description | Abstract The transport of circovirus capsid protein into nucleus is essential for viral replication in infected cell. However, the role of nucleolar shuttle proteins during porcine circovirus 3 capsid protein (PCV3 Cap) import is still not understood. Here, we report a previously unidentified nucleolar localization signal (NoLS) of PCV3 Cap, which hijacks the nucleolar phosphoprotein nucleophosmin-1 (NPM1) to facilitate nucleolar localization of PCV3 Cap. The NoLS of PCV3 Cap and serine-48 residue of N-terminal oligomerization domain of NPM1 are essential for PCV3 Cap/NPM1 interaction. In addition, charge property of serine-48 residue of NPM1 is critical for nucleolar localization and interaction with PCV3 Cap. Taken together, our findings demonstrate for the first time that NPM1 interacts with PCV3 Cap and is responsible for its nucleolar localization. |
| first_indexed | 2024-12-14T23:48:43Z |
| format | Article |
| id | doaj.art-e4f0f3248eea4a62b8fb090c633e2cf6 |
| institution | Directory Open Access Journal |
| issn | 1297-9716 |
| language | English |
| last_indexed | 2024-12-14T23:48:43Z |
| publishDate | 2021-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Veterinary Research |
| spelling | doaj.art-e4f0f3248eea4a62b8fb090c633e2cf62022-12-21T22:43:19ZengBMCVeterinary Research1297-97162021-01-0152111710.1186/s13567-020-00876-9The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid proteinJianwei Zhou0Juan Li1Haimin Li2Ying Zhang3Weiren Dong4Yulan Jin5Yan Yan6Jinyan Gu7Jiyong Zhou8MOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityMOA Key Laboratory of Animal Virology, Center of Veterinary Sciences, Zhejiang UniversityAbstract The transport of circovirus capsid protein into nucleus is essential for viral replication in infected cell. However, the role of nucleolar shuttle proteins during porcine circovirus 3 capsid protein (PCV3 Cap) import is still not understood. Here, we report a previously unidentified nucleolar localization signal (NoLS) of PCV3 Cap, which hijacks the nucleolar phosphoprotein nucleophosmin-1 (NPM1) to facilitate nucleolar localization of PCV3 Cap. The NoLS of PCV3 Cap and serine-48 residue of N-terminal oligomerization domain of NPM1 are essential for PCV3 Cap/NPM1 interaction. In addition, charge property of serine-48 residue of NPM1 is critical for nucleolar localization and interaction with PCV3 Cap. Taken together, our findings demonstrate for the first time that NPM1 interacts with PCV3 Cap and is responsible for its nucleolar localization.https://doi.org/10.1186/s13567-020-00876-9porcine circovirus type 3capsid proteinnucleolar localization signalnucleolar phosphoprotein nucleophosmin-1amino acid charge property |
| spellingShingle | Jianwei Zhou Juan Li Haimin Li Ying Zhang Weiren Dong Yulan Jin Yan Yan Jinyan Gu Jiyong Zhou The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein Veterinary Research porcine circovirus type 3 capsid protein nucleolar localization signal nucleolar phosphoprotein nucleophosmin-1 amino acid charge property |
| title | The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| title_full | The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| title_fullStr | The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| title_full_unstemmed | The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| title_short | The serine-48 residue of nucleolar phosphoprotein nucleophosmin-1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| title_sort | serine 48 residue of nucleolar phosphoprotein nucleophosmin 1 plays critical role in subcellular localization and interaction with porcine circovirus type 3 capsid protein |
| topic | porcine circovirus type 3 capsid protein nucleolar localization signal nucleolar phosphoprotein nucleophosmin-1 amino acid charge property |
| url | https://doi.org/10.1186/s13567-020-00876-9 |
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