Proteomic Characterization of PAMs with PRRSV-ADE Infection
The antibody-dependent enhancement (ADE) effect of a PRRSV infection is that the preexisting sub- or non-neutralizing antibodies specific against PRRSV can facilitate the virus entry and replication, and it is likely to be a great obstacle for the selection of immune strategies and the development o...
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MDPI AG
2022-12-01
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author | Pengli Xu Wen Li Shijie Zhao Zhiying Cui Yu Chen Yi-na Zhang Jing Chen Pingan Xia |
author_facet | Pengli Xu Wen Li Shijie Zhao Zhiying Cui Yu Chen Yi-na Zhang Jing Chen Pingan Xia |
author_sort | Pengli Xu |
collection | DOAJ |
description | The antibody-dependent enhancement (ADE) effect of a PRRSV infection is that the preexisting sub- or non-neutralizing antibodies specific against PRRSV can facilitate the virus entry and replication, and it is likely to be a great obstacle for the selection of immune strategies and the development of high-efficiency PRRSV vaccines. However, the proteomic characterization of primary alveolar macrophages (PAMs) with a PRRSV-ADE infection has not yet been investigated so far. Therefore, we performed a tandem mass tag (TMT)-based quantitative proteomic analysis of PAMs with a PRRSV-ADE infection in this study. The results showed that a total of 3935 differentially expressed proteins (DEPs) were identified in the PAMs infected with PRRSV-ADE, including 2004 up-regulated proteins and 1931 down-regulated proteins. Further, the bioinformatics analysis for these DEPs revealed that a PRRSV-ADE infection might disturb the functions of ribosome, proteasome and mitochondria. Interestingly, we also found that the expression of the key molecules in the innate immune pathways and antiviral proteins were significantly down-regulated during a PRRSV-ADE infection. This study was the first attempt to analyze the proteomic characterization of PAMs with a PRRSV-ADE infection in vitro. Additionally, the findings will provide valuable information for a better understanding of the mechanism of virus–antibody–host interactions during a PRRSV-ADE infection. |
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institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-09T11:03:36Z |
publishDate | 2022-12-01 |
publisher | MDPI AG |
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series | Viruses |
spelling | doaj.art-d4afc977ac644dfb849dadbee21beef72023-12-01T01:06:51ZengMDPI AGViruses1999-49152022-12-011513610.3390/v15010036Proteomic Characterization of PAMs with PRRSV-ADE InfectionPengli Xu0Wen Li1Shijie Zhao2Zhiying Cui3Yu Chen4Yi-na Zhang5Jing Chen6Pingan Xia7College 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, ChinaThe antibody-dependent enhancement (ADE) effect of a PRRSV infection is that the preexisting sub- or non-neutralizing antibodies specific against PRRSV can facilitate the virus entry and replication, and it is likely to be a great obstacle for the selection of immune strategies and the development of high-efficiency PRRSV vaccines. However, the proteomic characterization of primary alveolar macrophages (PAMs) with a PRRSV-ADE infection has not yet been investigated so far. Therefore, we performed a tandem mass tag (TMT)-based quantitative proteomic analysis of PAMs with a PRRSV-ADE infection in this study. The results showed that a total of 3935 differentially expressed proteins (DEPs) were identified in the PAMs infected with PRRSV-ADE, including 2004 up-regulated proteins and 1931 down-regulated proteins. Further, the bioinformatics analysis for these DEPs revealed that a PRRSV-ADE infection might disturb the functions of ribosome, proteasome and mitochondria. Interestingly, we also found that the expression of the key molecules in the innate immune pathways and antiviral proteins were significantly down-regulated during a PRRSV-ADE infection. This study was the first attempt to analyze the proteomic characterization of PAMs with a PRRSV-ADE infection in vitro. Additionally, the findings will provide valuable information for a better understanding of the mechanism of virus–antibody–host interactions during a PRRSV-ADE infection.https://www.mdpi.com/1999-4915/15/1/36PRRSVPRRSV-ADE infectionPAMsproteomicsvirus–antibody–host interactions |
spellingShingle | Pengli Xu Wen Li Shijie Zhao Zhiying Cui Yu Chen Yi-na Zhang Jing Chen Pingan Xia Proteomic Characterization of PAMs with PRRSV-ADE Infection Viruses PRRSV PRRSV-ADE infection PAMs proteomics virus–antibody–host interactions |
title | Proteomic Characterization of PAMs with PRRSV-ADE Infection |
title_full | Proteomic Characterization of PAMs with PRRSV-ADE Infection |
title_fullStr | Proteomic Characterization of PAMs with PRRSV-ADE Infection |
title_full_unstemmed | Proteomic Characterization of PAMs with PRRSV-ADE Infection |
title_short | Proteomic Characterization of PAMs with PRRSV-ADE Infection |
title_sort | proteomic characterization of pams with prrsv ade infection |
topic | PRRSV PRRSV-ADE infection PAMs proteomics virus–antibody–host interactions |
url | https://www.mdpi.com/1999-4915/15/1/36 |
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