Acta Veterinaria et Zootechnica Sinica ›› 2024, Vol. 55 ›› Issue (6): 2540-2549.doi: 10.11843/j.issn.0366-6964.2024.06.025

• Preventive Veterinary Medicine • Previous Articles     Next Articles

Regulation of Heat Shock Protein 27 on the Proliferation of Vesicular Stomatitis Virus in vitro

Dianyu LI1,2(), Rongqian MO1,2, Xu ZHAO2, Ming GAO2, Hongshan LI1,2, Huisheng BAI2, Ruixian MA1,2, Xiangrong LI1,3,*(), Ruofei FENG1,3,*()   

  1. 1. Key Laboratory of Biotechnology and Bioengineering of State Ethnic Affairs Commission, Biomedical Research Center, Northwest Minzu University, Lanzhou 730030, China
    2. Life Science and Engineering College of Northwest Minzu University, Lanzhou 730030, China
    3. Engineering Research Center of Key Technology and Industrialization of Cell-based Vaccine, Ministry of Education, Biomedical Research Center, Northwest Minzu University, Lanzhou 730030, China
  • Received:2023-06-26 Online:2024-06-23 Published:2024-06-28
  • Contact: Xiangrong LI, Ruofei FENG E-mail:994398211@qq.com;lixiangrong@xbmu.edu.cn;fengruofei@xbmu.edu.cn

Abstract:

This study was conducted to investigate the effect and mechanism of heat shock protein 27 (HSP27) on the proliferation of vesicular stomatitis virus (VSV) in vitro and the retinoid acid-inducible gene-I-like receptor (RLR) signaling pathway mediated by VSV infection. Real-time quantitative PCR, Western blotting, Co-immunoprecipitation, TCID50 assay, and immunofluorescence methods were employed to reveal the effects of VSV infection on the mRNA and protein expression of HSP27, and then the effects of overexpression and interference with HSP27 on the proliferation of VSV, and further explore the effects of HSP27 on the RLR signaling pathway mediated by VSV infection. Finally, the interaction and co-localization between HSP27 and the target molecules in RLR signaling pathway were analyzed. The results showed that VSV infection could increase the gene transcription and protein expression of HSP27, both stable and transient overexpression of HSP27 significantly inhibited the proliferation of VSV in vitro. Interfering with HSP27 expression in host cells promoted the proliferation of VSV. Further studies showed that HSP27 enhanced both VSV and retinoic acid-inducible gene I protein (RIG-I) mediated IFN-β production and the protein expression of RIG-I, and that HSP27 interacted with RIG-I and co-localized in the cytoplasm. This study for the revealed the molecular mechanism by which HSP27 targets RIG-I to upregulate its expression, enhance the transduction of RLR signaling pathways, and then negatively regulate the proliferation of VSV in vitro, laying a foundation for further revealing the mechanism of host factor HSP27 in viral infection.

Key words: heat shock protein 27, vesicular stomatitis virus, RLR signaling pathway, RIG-I

CLC Number: