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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...

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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2019
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
Descripción
Sumario: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.