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PRRSV Induces HMGB1 Phosphorylation at Threonine-51 Residue to Enhance Its Secretion.
Wang, Rong; Zhang, Jingyi; Fu, Yu; Jia, Linying; Zhang, Yali; Bai, Liang; Wang, Weirong; Cheng, Daxin; Liu, Enqi.
Afiliación
  • Wang R; Laboratory Animal Center, Xi'an Jiaotong University, Xi'an 710061, China.
  • Zhang J; Department of Laboratory Animal Science, School of Basic Medical Sciences, Xi'an Jiaotong University, Xi'an 710061, China.
  • Fu Y; Laboratory Animal Center, Xi'an Jiaotong University, Xi'an 710061, China.
  • Jia L; Department of Laboratory Animal Science, School of Basic Medical Sciences, Xi'an Jiaotong University, Xi'an 710061, China.
  • Zhang Y; Laboratory Animal Center, Xi'an Jiaotong University, Xi'an 710061, China.
  • Bai L; Department of Laboratory Animal Science, School of Basic Medical Sciences, Xi'an Jiaotong University, Xi'an 710061, China.
  • Wang W; Laboratory Animal Center, Xi'an Jiaotong University, Xi'an 710061, China.
  • Cheng D; Department of Laboratory Animal Science, School of Basic Medical Sciences, Xi'an Jiaotong University, Xi'an 710061, China.
  • Liu E; Laboratory Animal Center, Xi'an Jiaotong University, Xi'an 710061, China.
Viruses ; 14(5)2022 05 08.
Article en En | MEDLINE | ID: mdl-35632744
Porcine reproductive and respiratory syndrome virus (PRRSV) induces secretion of high mobility group box 1 (HMGB1) to mediate inflammatory response that is involved in the pulmonary injury of infected pigs. Our previous study indicates that protein kinase C-delta (PKC-delta) is essential for HMGB1 secretion in PRRSV-infected cells. However, the underlying mechanism in HMGB1 secretion induced by PRRSV infection is still unclear. Here, we discovered that the phosphorylation level of HMGB1 in threonine residues increased in PRRSV-infected cells. A site-directed mutagenesis study showed that HMGB1 phosphorylation at threonine-51 was associated with HMGB1 secretion induced by PRRSV infection. Co-immunoprecipitation (co-IP) of HMGB1 failed to precipitate PKC-delta, but interestingly, mass spectrometry analysis of the HMGB1 co-IP product showed that PRRSV infection enhanced HMGB1 binding to ribosomal protein S3 (RPS3), which has various extra-ribosomal functions. The silencing of RPS3 by siRNA blocked HMGB1 secretion induced by PRRSV infection. Moreover, the phosphorylation of HMGB1 at threonine-51 was correlated with the interaction between HMGB1 and RPS3. In vivo, PRRSV infection also increased RPS3 levels and nuclear accumulation in pulmonary alveolar macrophages. These results demonstrate that PRRSV may induce HMGB1 phosphorylation at threonine-51 and increase its interaction with RPS3 to enhance HMGB1 secretion. This finding provides insights into the pathogenesis of PRRSV infection.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Virus del Síndrome Respiratorio y Reproductivo Porcino / Síndrome Respiratorio y de la Reproducción Porcina / Proteína HMGB1 Límite: Animals Idioma: En Revista: Viruses Año: 2022 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Virus del Síndrome Respiratorio y Reproductivo Porcino / Síndrome Respiratorio y de la Reproducción Porcina / Proteína HMGB1 Límite: Animals Idioma: En Revista: Viruses Año: 2022 Tipo del documento: Article País de afiliación: China