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The phosphorylation of the N protein could affect PRRSV virulence in vivo
The porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is a multiphosphorylated protein.It has been proved that the phosphorylation of N protein could regulate the growth ability of PRRSV in Marc-145 cells. However, further investigation is needed to determine wheth...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7117339/ https://www.ncbi.nlm.nih.gov/pubmed/30955814 http://dx.doi.org/10.1016/j.vetmic.2019.03.018 |
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author | Chen, Yao Yu, Zhiqing Yi, Heyou Wei, Yingfang Han, Xiaoliang Li, Qi Ji, Chihai Huang, Junmin Deng, Qiwei Liu, Yixin Cai, Mengkai He, Shuyi Ma, Chunquan Zhang, Guihong |
author_facet | Chen, Yao Yu, Zhiqing Yi, Heyou Wei, Yingfang Han, Xiaoliang Li, Qi Ji, Chihai Huang, Junmin Deng, Qiwei Liu, Yixin Cai, Mengkai He, Shuyi Ma, Chunquan Zhang, Guihong |
author_sort | Chen, Yao |
collection | PubMed |
description | The porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is a multiphosphorylated protein.It has been proved that the phosphorylation of N protein could regulate the growth ability of PRRSV in Marc-145 cells. However, further investigation is needed to determine whether phosphorylation of the N protein could affect PRRSV virulence in piglets. In this study, we confirmed that the mutations could impair PRRSV replication ability in porcine primary macrophages (PAMs) as they did in Marc-145 cells. The animal experiments suggested that the pathogenicity of the mutated virus (A105-120) was significantly reduced compared with parent strain (XH-GD). Our results suggested that the phosphorylation of the N protein contributes to virus replication and virulence. This study is the first to identify a specific modification involved in PRRSV pathogenicity. Mutation of PTMs sites is also a novel way to attenuate PRRSV virulence. The mutations could be a marker in a vaccine. In conclusion, our study will improve our understanding of the molecular mechanisms of PRRSV pathogenicity. |
format | Online Article Text |
id | pubmed-7117339 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71173392020-04-02 The phosphorylation of the N protein could affect PRRSV virulence in vivo Chen, Yao Yu, Zhiqing Yi, Heyou Wei, Yingfang Han, Xiaoliang Li, Qi Ji, Chihai Huang, Junmin Deng, Qiwei Liu, Yixin Cai, Mengkai He, Shuyi Ma, Chunquan Zhang, Guihong Vet Microbiol Article The porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is a multiphosphorylated protein.It has been proved that the phosphorylation of N protein could regulate the growth ability of PRRSV in Marc-145 cells. However, further investigation is needed to determine whether phosphorylation of the N protein could affect PRRSV virulence in piglets. In this study, we confirmed that the mutations could impair PRRSV replication ability in porcine primary macrophages (PAMs) as they did in Marc-145 cells. The animal experiments suggested that the pathogenicity of the mutated virus (A105-120) was significantly reduced compared with parent strain (XH-GD). Our results suggested that the phosphorylation of the N protein contributes to virus replication and virulence. This study is the first to identify a specific modification involved in PRRSV pathogenicity. Mutation of PTMs sites is also a novel way to attenuate PRRSV virulence. The mutations could be a marker in a vaccine. In conclusion, our study will improve our understanding of the molecular mechanisms of PRRSV pathogenicity. Elsevier B.V. 2019-04 2019-03-14 /pmc/articles/PMC7117339/ /pubmed/30955814 http://dx.doi.org/10.1016/j.vetmic.2019.03.018 Text en © 2019 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Chen, Yao Yu, Zhiqing Yi, Heyou Wei, Yingfang Han, Xiaoliang Li, Qi Ji, Chihai Huang, Junmin Deng, Qiwei Liu, Yixin Cai, Mengkai He, Shuyi Ma, Chunquan Zhang, Guihong The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title | The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title_full | The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title_fullStr | The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title_full_unstemmed | The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title_short | The phosphorylation of the N protein could affect PRRSV virulence in vivo |
title_sort | phosphorylation of the n protein could affect prrsv virulence in vivo |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7117339/ https://www.ncbi.nlm.nih.gov/pubmed/30955814 http://dx.doi.org/10.1016/j.vetmic.2019.03.018 |
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