Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication
Avian reovirus (ARV) is highly prevalent in healthy poultry flocks and has been linked to viral arthritis/tendonitis, dwarf syndrome, chronic respiratory disease, and immunosuppression in avian species, resulting in significant economic losses within the poultry industry. The non-structural protein...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-01-01
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| Series: | Poultry Science |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S003257912401160X |
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| author | Hu Xiaomiao Zhao Ruihong Li Wei Pan Xiaocheng Dai Yin Wu Huimin Wu Yantao Zhang Chengcheng |
| author_facet | Hu Xiaomiao Zhao Ruihong Li Wei Pan Xiaocheng Dai Yin Wu Huimin Wu Yantao Zhang Chengcheng |
| author_sort | Hu Xiaomiao |
| collection | DOAJ |
| description | Avian reovirus (ARV) is highly prevalent in healthy poultry flocks and has been linked to viral arthritis/tendonitis, dwarf syndrome, chronic respiratory disease, and immunosuppression in avian species, resulting in significant economic losses within the poultry industry. The non-structural protein p17 encoded by ARV induces cellular autophagy and facilitates viral proliferation, playing a pivotal role in viral pathogenesis. To further elucidate the pathogenic mechanism basis of ARV p17 protein function, we employed a yeast two-hybrid system to identify Phosphoribosyl pyrophosphate synthetase 2 (PRPS2) as an interacting host protein with p17. In this study, we validated the interaction between PRPS2 and p17 using laser confocal microscopy, coimmunoprecipitation, and GST-Pulldown assays. Moreover, our findings demonstrate that the C-terminal region of PRPS2 is responsible for its binding to the p17 protein. Intriguingly, ARV infection significantly upregulated PRPS2 expression levels. Additionally, PRPS2 was shown to have a substantial impact on ARV replication; overexpression of PRPS2 increased ARV replication while knockdown of PRPS2 resulted in decreased quantities of ARV particles. Furthermore, our findings suggest that this process involves cellular apoptosis as a potential mechanism underlying these observations. Overall, this research provides valuable insights into elucidating the function of the p17 protein and sheds light on the pathogenic mechanism involving ARV-induced cellular apoptosis while offering novel perspectives for exploring therapeutic targets against ARV. |
| format | Article |
| id | doaj-art-6e692afa473b4f1783ea164b7b221440 |
| institution | Kabale University |
| issn | 0032-5791 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Poultry Science |
| spelling | doaj-art-6e692afa473b4f1783ea164b7b2214402025-01-22T05:40:34ZengElsevierPoultry Science0032-57912025-01-011041104582Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replicationHu Xiaomiao0Zhao Ruihong1Li Wei2Pan Xiaocheng3Dai Yin4Wu Huimin5Wu Yantao6Zhang Chengcheng7Institute of Animal Husbandry and Veterinary Medicine, Anhui Academy of Agricultural Sciences/Livestock and Poultry Epidemic Diseases Research Center of Anhui Province/Anhui province Key laboratory of Livestock and Poultry Product Safety Engineering, Hefei, Anhui 230031, ChinaInstitute of Animal Husbandry and Veterinary Medicine, Anhui Academy of Agricultural Sciences/Livestock and Poultry Epidemic Diseases Research Center of Anhui Province/Anhui province Key laboratory of Livestock and Poultry Product Safety Engineering, Hefei, Anhui 230031, ChinaYangzhou Polytechnic College, Yangzhou 225009, ChinaInstitute of Animal Husbandry and Veterinary Medicine, Anhui Academy of Agricultural Sciences/Livestock and Poultry Epidemic Diseases Research Center of Anhui Province/Anhui province Key laboratory of Livestock and Poultry Product Safety Engineering, Hefei, Anhui 230031, ChinaInstitute of Animal Husbandry and Veterinary Medicine, Anhui Academy of Agricultural Sciences/Livestock and Poultry Epidemic Diseases Research Center of Anhui Province/Anhui province Key laboratory of Livestock and Poultry Product Safety Engineering, Hefei, Anhui 230031, ChinaCollege of Veterinary Medicine, Yangzhou University, Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, Jiangsu 225009, PR ChinaCollege of Veterinary Medicine, Yangzhou University, Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, Jiangsu 225009, PR ChinaCollege of Veterinary Medicine, Yangzhou University, Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, Jiangsu 225009, PR China; Corresponding author.Avian reovirus (ARV) is highly prevalent in healthy poultry flocks and has been linked to viral arthritis/tendonitis, dwarf syndrome, chronic respiratory disease, and immunosuppression in avian species, resulting in significant economic losses within the poultry industry. The non-structural protein p17 encoded by ARV induces cellular autophagy and facilitates viral proliferation, playing a pivotal role in viral pathogenesis. To further elucidate the pathogenic mechanism basis of ARV p17 protein function, we employed a yeast two-hybrid system to identify Phosphoribosyl pyrophosphate synthetase 2 (PRPS2) as an interacting host protein with p17. In this study, we validated the interaction between PRPS2 and p17 using laser confocal microscopy, coimmunoprecipitation, and GST-Pulldown assays. Moreover, our findings demonstrate that the C-terminal region of PRPS2 is responsible for its binding to the p17 protein. Intriguingly, ARV infection significantly upregulated PRPS2 expression levels. Additionally, PRPS2 was shown to have a substantial impact on ARV replication; overexpression of PRPS2 increased ARV replication while knockdown of PRPS2 resulted in decreased quantities of ARV particles. Furthermore, our findings suggest that this process involves cellular apoptosis as a potential mechanism underlying these observations. Overall, this research provides valuable insights into elucidating the function of the p17 protein and sheds light on the pathogenic mechanism involving ARV-induced cellular apoptosis while offering novel perspectives for exploring therapeutic targets against ARV.http://www.sciencedirect.com/science/article/pii/S003257912401160XAvian reovirusp17 proteinPRPS2Replication |
| spellingShingle | Hu Xiaomiao Zhao Ruihong Li Wei Pan Xiaocheng Dai Yin Wu Huimin Wu Yantao Zhang Chengcheng Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication Poultry Science Avian reovirus p17 protein PRPS2 Replication |
| title | Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication |
| title_full | Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication |
| title_fullStr | Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication |
| title_full_unstemmed | Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication |
| title_short | Host protein PRPS2 interact with the non-structural protein p17 of Avian Reovirus and promote viral replication |
| title_sort | host protein prps2 interact with the non structural protein p17 of avian reovirus and promote viral replication |
| topic | Avian reovirus p17 protein PRPS2 Replication |
| url | http://www.sciencedirect.com/science/article/pii/S003257912401160X |
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