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Updated: Jan 17, 2026

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
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siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells

Published on: October 28, 2019

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Cytoplasmic translocation of tripartite motif-containing 28 is critical for PRRSV-induced autophagy through promoting

Meng Chen1,2, Yuna Zhao1, Hui An1

  • 1Shandong Provincial Key Laboratory of Zoonoses, College of Veterinary Medicine, Shandong Agricultural University, Taian, Shandong, China.

Journal of Virology
|September 24, 2025
PubMed

Insights

Porcine reproductive and respiratory syndrome virus (PRRSV) hijacks the host protein TRIM28 to trigger autophagy, a cellular process that can aid viral replication. This study uncovers the Nsp4 protein

Area of Science:

  • Virology
  • Cellular Biology
  • Immunology

Background:

  • Autophagy plays a complex role in viral infections, including those caused by porcine reproductive and respiratory syndrome virus (PRRSV).
  • The interaction between PRRSV and autophagy-related factors like tripartite motif-containing 28 (TRIM28) is not fully understood.
  • PRRSV infection causes significant economic losses in the swine industry due to respiratory and reproductive issues.

Purpose of the Study:

  • To elucidate the mechanism by which PRRSV induces autophagy.
  • To investigate the role of TRIM28 in PRRSV-mediated autophagy.
  • To identify viral components responsible for initiating autophagy during PRRSV infection.

Main Methods:

  • Investigated dynamic changes in autophagy and TRIM28 during PRRSV infection in vitro and in vivo.
  • Utilized a CRM1-dependent pathway assay to track TRIM28 nuclear export.
  • Examined the interaction between TRIM28, Vps34, and Beclin1 to assess Vps34-Beclin1 complex formation.

Main Results:

  • PRRSV Nsp4 protein mediates the nuclear export of TRIM28 through a CRM1-dependent pathway.
  • Cytoplasmic TRIM28 promotes the formation of the Vps34-Beclin1 complex, initiating autophagy.
  • TRIM28 exhibits antiviral properties, though the exact mechanism requires further investigation.

Conclusions:

  • PRRSV Nsp4 is a key viral factor that triggers autophagy by inducing TRIM28 nuclear export.
  • TRIM28 plays a crucial role in initiating PRRSV-mediated autophagy by facilitating Vps34-Beclin1 complex formation.
  • This study provides novel insights into PRRSV pathogenesis and suggests potential targets for antiviral drug development.
Keywords:
CRM1-dependent pathwayPRRSVTRIM28autophagy

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