Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs
Porcine reproductive and respiratory syndrome virus (PRRSV) is a typical immunosuppressive virus causing a large economic impact on the swine industry. The structural protein GP5 of PRRSV plays a pivotal role in its pathogenicity and immune evasion. Virus–host interactions play a crucial part in vir...
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MDPI AG
2024-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/25/5/2778 |
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| author | Wen Li Yueshuai Wang Mengting Zhang Shijie Zhao Mengxiang Wang Ruijie Zhao Jing Chen Yina Zhang Pingan Xia |
| author_facet | Wen Li Yueshuai Wang Mengting Zhang Shijie Zhao Mengxiang Wang Ruijie Zhao Jing Chen Yina Zhang Pingan Xia |
| author_sort | Wen Li |
| collection | DOAJ |
| description | Porcine reproductive and respiratory syndrome virus (PRRSV) is a typical immunosuppressive virus causing a large economic impact on the swine industry. The structural protein GP5 of PRRSV plays a pivotal role in its pathogenicity and immune evasion. Virus–host interactions play a crucial part in viral replication and immune escape. Therefore, understanding the interactions between GP5 and host proteins are significant for porcine reproductive and respiratory syndrome (PRRS) control. However, the interaction network between GP5 and host proteins in primary porcine alveolar macrophages (PAMs) has not been reported. In this study, 709 GP5-interacting host proteins were identified in primary PAMs by immunoprecipitation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS). Bioinformatics analysis revealed that these proteins were involved in multiple cellular processes, such as translation, protein transport, and protein stabilization. Subsequently, immunoprecipitation and immunofluorescence assay confirmed that GP5 could interact with antigen processing and presentation pathways related proteins. Finally, we found that GP5 may be a key protein that inhibits the antigen processing and presentation pathway during PRRSV infection. The novel host proteins identified in this study will be the candidates for studying the biological functions of GP5, which will provide new insights into PRRS prevention and vaccine development. |
| first_indexed | 2024-04-25T00:29:17Z |
| format | Article |
| id | doaj.art-ae8c985343214051a050865b652ca080 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-04-25T00:29:17Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-ae8c985343214051a050865b652ca0802024-03-12T16:46:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-02-01255277810.3390/ijms25052778Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMsWen Li0Yueshuai Wang1Mengting Zhang2Shijie Zhao3Mengxiang Wang4Ruijie Zhao5Jing Chen6Yina Zhang7Pingan Xia8College of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Life Science, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaCollege of Veterinary Medicine, Henan Agricultural University, Longzi Lake 15#, Zhengzhou 450046, ChinaPorcine reproductive and respiratory syndrome virus (PRRSV) is a typical immunosuppressive virus causing a large economic impact on the swine industry. The structural protein GP5 of PRRSV plays a pivotal role in its pathogenicity and immune evasion. Virus–host interactions play a crucial part in viral replication and immune escape. Therefore, understanding the interactions between GP5 and host proteins are significant for porcine reproductive and respiratory syndrome (PRRS) control. However, the interaction network between GP5 and host proteins in primary porcine alveolar macrophages (PAMs) has not been reported. In this study, 709 GP5-interacting host proteins were identified in primary PAMs by immunoprecipitation coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS). Bioinformatics analysis revealed that these proteins were involved in multiple cellular processes, such as translation, protein transport, and protein stabilization. Subsequently, immunoprecipitation and immunofluorescence assay confirmed that GP5 could interact with antigen processing and presentation pathways related proteins. Finally, we found that GP5 may be a key protein that inhibits the antigen processing and presentation pathway during PRRSV infection. The novel host proteins identified in this study will be the candidates for studying the biological functions of GP5, which will provide new insights into PRRS prevention and vaccine development.https://www.mdpi.com/1422-0067/25/5/2778PRRSVGP5LC-MS/MSprotein–protein interactionantigen processing and presentation |
| spellingShingle | Wen Li Yueshuai Wang Mengting Zhang Shijie Zhao Mengxiang Wang Ruijie Zhao Jing Chen Yina Zhang Pingan Xia Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs International Journal of Molecular Sciences PRRSV GP5 LC-MS/MS protein–protein interaction antigen processing and presentation |
| title | Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs |
| title_full | Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs |
| title_fullStr | Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs |
| title_full_unstemmed | Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs |
| title_short | Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs |
| title_sort | mass spectrometry based proteomic analysis of potential host proteins interacting with gp5 in prrsv infected pams |
| topic | PRRSV GP5 LC-MS/MS protein–protein interaction antigen processing and presentation |
| url | https://www.mdpi.com/1422-0067/25/5/2778 |
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