DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage
Abstract In herpesvirus, the terminase subunit pUL15 is involved in cleavage of the viral genome concatemers in the nucleus. Previous studies have shown that herpes simplex virus 1 (HSV-1) pUL15 can enter the nucleus without other viral proteins and help other terminase subunits enter the nucleus. H...
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BMC
2025-01-01
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| Series: | Veterinary Research |
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| Online Access: | https://doi.org/10.1186/s13567-024-01420-9 |
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| author | Qiao Yang Yaya Feng Lizhen Liu Linlin Yang Mingshu Wang Ying Wu Bin Tian Xumin Ou Renyong Jia Dekang Zhu Shun Chen Mafeng Liu Xinxin Zhao Shaqiu Zhang Juan Huang Di Sun Yu He Zhen Wu Ling Zhang Yanling Yu Anchun Cheng |
| author_facet | Qiao Yang Yaya Feng Lizhen Liu Linlin Yang Mingshu Wang Ying Wu Bin Tian Xumin Ou Renyong Jia Dekang Zhu Shun Chen Mafeng Liu Xinxin Zhao Shaqiu Zhang Juan Huang Di Sun Yu He Zhen Wu Ling Zhang Yanling Yu Anchun Cheng |
| author_sort | Qiao Yang |
| collection | DOAJ |
| description | Abstract In herpesvirus, the terminase subunit pUL15 is involved in cleavage of the viral genome concatemers in the nucleus. Previous studies have shown that herpes simplex virus 1 (HSV-1) pUL15 can enter the nucleus without other viral proteins and help other terminase subunits enter the nucleus. However, this study revealed that duck plague virus (DPV) pUL15 cannot localize independently to the nucleus and can only be localized in the nucleus in the presence of pUL28 and pUL33. However, the data suggested the presence of a potential nuclear localization signal (NLS) in DPV pUL15, which is important for the localization of the terminase subunits. Subsequently, several single-point mutants were constructed to identify the vital amino acids within the NLS. The conserved amino acids K187, R188, and K190 are critical for the nuclear localization of pUL15, pUL28, and pUL33 but not for their interaction. Furthermore, corresponding recombinant viruses were constructed. The results revealed that the mutations rUL15K187Q, rUL15K188Q and rUL15K190Q had an obvious influence on concatemeric genome cleavage, but only K190Q significantly affected the production of progeny virions. These findings indicate that the NLS is important for the functions of DPV pUL15. Overall, a potential NLS and the key amino acids in DPV pUL15 were identified. Mutations in K187, K188 and K190 affected the cleavage of the concatemeric genome, but only mutations in K190 had an obvious effect on viral proliferation. |
| format | Article |
| id | doaj-art-faafed546bc74beda929dbfad792189a |
| institution | Kabale University |
| issn | 1297-9716 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Veterinary Research |
| spelling | doaj-art-faafed546bc74beda929dbfad792189a2025-01-12T12:35:27ZengBMCVeterinary Research1297-97162025-01-0156111410.1186/s13567-024-01420-9DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavageQiao Yang0Yaya Feng1Lizhen Liu2Linlin Yang3Mingshu Wang4Ying Wu5Bin Tian6Xumin Ou7Renyong Jia8Dekang Zhu9Shun Chen10Mafeng Liu11Xinxin Zhao12Shaqiu Zhang13Juan Huang14Di Sun15Yu He16Zhen Wu17Ling Zhang18Yanling Yu19Anchun Cheng20Engineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationEngineering Research Center of Southwest Animal Disease Prevention and Control Technology, Ministry of EducationAbstract In herpesvirus, the terminase subunit pUL15 is involved in cleavage of the viral genome concatemers in the nucleus. Previous studies have shown that herpes simplex virus 1 (HSV-1) pUL15 can enter the nucleus without other viral proteins and help other terminase subunits enter the nucleus. However, this study revealed that duck plague virus (DPV) pUL15 cannot localize independently to the nucleus and can only be localized in the nucleus in the presence of pUL28 and pUL33. However, the data suggested the presence of a potential nuclear localization signal (NLS) in DPV pUL15, which is important for the localization of the terminase subunits. Subsequently, several single-point mutants were constructed to identify the vital amino acids within the NLS. The conserved amino acids K187, R188, and K190 are critical for the nuclear localization of pUL15, pUL28, and pUL33 but not for their interaction. Furthermore, corresponding recombinant viruses were constructed. The results revealed that the mutations rUL15K187Q, rUL15K188Q and rUL15K190Q had an obvious influence on concatemeric genome cleavage, but only K190Q significantly affected the production of progeny virions. These findings indicate that the NLS is important for the functions of DPV pUL15. Overall, a potential NLS and the key amino acids in DPV pUL15 were identified. Mutations in K187, K188 and K190 affected the cleavage of the concatemeric genome, but only mutations in K190 had an obvious effect on viral proliferation.https://doi.org/10.1186/s13567-024-01420-9DPVterminasePUL15NLSgenome cleavage |
| spellingShingle | Qiao Yang Yaya Feng Lizhen Liu Linlin Yang Mingshu Wang Ying Wu Bin Tian Xumin Ou Renyong Jia Dekang Zhu Shun Chen Mafeng Liu Xinxin Zhao Shaqiu Zhang Juan Huang Di Sun Yu He Zhen Wu Ling Zhang Yanling Yu Anchun Cheng DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage Veterinary Research DPV terminase PUL15 NLS genome cleavage |
| title | DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| title_full | DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| title_fullStr | DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| title_full_unstemmed | DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| title_short | DPV pUL15 possesses a potential NLS, which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| title_sort | dpv pul15 possesses a potential nls which is important for the location of the terminase complex and for viral proliferation and genome cleavage |
| topic | DPV terminase PUL15 NLS genome cleavage |
| url | https://doi.org/10.1186/s13567-024-01420-9 |
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