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Stimulation of Cytoplasmic DNA Sensing Pathways In Vitro and In Vivo
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TRIM30α Is a Negative-Feedback Regulator of the Intracellular DNA and DNA Virus-Triggered Response by Targeting STING

Yanming Wang1, Qiaoshi Lian2, Bo Yang3

  • 1Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China; School of Life Sciences, University of Science and Technology of China, Hefei, China.

Plos Pathogens
|June 27, 2015
PubMed

Insights

The E3 ubiquitin ligase TRIM30α negatively regulates innate immune responses to DNA viruses. It targets STING (stimulator of interferon genes) for degradation, controlling autoimmune disease risk.

Area of Science:

  • Immunology
  • Molecular Biology
  • Virology

Background:

  • Uncontrolled immune responses to intracellular DNA can trigger autoimmune diseases.
  • Maintaining immune homeostasis against cytosolic DNA is vital for host survival and preventing autoimmunity.
  • Dendritic cells (DCs) play a crucial role in initiating immune responses to pathogens like DNA viruses.

Purpose of the Study:

  • To investigate the role of E3 ubiquitin ligase tripartite motif protein 30α (TRIM30α) in regulating innate immune responses to DNA viruses.
  • To elucidate the mechanism by which TRIM30α modulates the DNA-sensing pathway.
  • To determine the impact of TRIM30α on host defense against DNA virus infections.

Main Methods:

  • Herpes simplex virus type 1 (HSV-1) infection of dendritic cells (DCs).
  • Knockdown and genetic ablation of TRIM30α in cells and mice.
  • Biochemical analyses including protein interaction and ubiquitination assays.
  • Proteasome activity assays to assess protein degradation pathways.

Main Results:

  • TRIM30α expression was induced by HSV-1 infection in DCs.
  • TRIM30α deficiency enhanced type I Interferon (IFN) and interleukin-6 responses to intracellular DNA and DNA viruses.
  • TRIM30α-deficient mice exhibited increased resistance to DNA virus infections.
  • TRIM30α directly interacted with STING and promoted its degradation via K48-linked ubiquitination at Lys275, dependent on the proteasome pathway.

Conclusions:

  • TRIM30α acts as a negative-feedback regulator of innate immunity against DNA viruses.
  • TRIM30α targets STING for proteasomal degradation, thereby dampening the DNA-sensing pathway.
  • TRIM30α plays a critical role in controlling immune responses to DNA viruses and preventing autoimmunity.

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