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Crystal structure and functional implication of bacterial STING.

Tzu-Ping Ko1, Yu-Chuan Wang2, Chia-Shin Yang2

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|January 11, 2022
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Bacterial STING senses cyclic-di-GMP during phage infection, triggering cell suicide to limit viral spread. Structural analysis reveals precise c-di-GMP binding and bacterial STING filament formation mechanisms.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Immunology

Background:

  • Mammalian STING (Stimulator of Interferon Genes) is crucial for innate immunity.
  • Bacterial STING, an ancient homolog, plays a role in defense against phage infection.
  • The precise mechanism of bacterial STING's interaction with cyclic dinucleotides is not fully understood.

Purpose of the Study:

  • To elucidate the binding mode of cyclic-di-GMP (c-di-GMP) to bacterial STING.
  • To understand the structural basis for bacterial STING filament formation.
  • To explore the evolutionary relationship between bacterial and eukaryotic STING signaling.

Main Methods:

  • X-ray crystallography to determine complex structures of bacterial STING bound to c-di-GMP.
  • Analysis of protein-protein interactions to understand oligomerization.
  • Bioinformatic analysis to classify bacterial STING and infer evolutionary pathways.

Main Results:

  • Two crystal structures reveal how bacterial STING specifically binds c-di-GMP.
  • Protein-protein interactions driving bacterial STING filament formation were identified.
  • Bacterial STING proteins were classified into two groups based on a conserved motif, influencing ligand specificity and oligomerization.

Conclusions:

  • Bacterial STING utilizes specific structural features to recognize c-di-GMP and form filaments.
  • These findings provide insights into the evolution of STING signaling from bacteria to eukaryotes.
  • The study clarifies the ancient function of STING in prokaryotic antiviral defense.