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Crystal structure and functional implication of bacterial STING

Author

Listed:
  • Tzu-Ping Ko

    (Institute of Biological Chemistry, Academia Sinica)

  • Yu-Chuan Wang

    (Institute of New Drug Development, China Medical University)

  • Chia-Shin Yang

    (Institute of New Drug Development, China Medical University)

  • Mei-Hui Hou

    (Institute of New Drug Development, China Medical University)

  • Chao-Jung Chen

    (Graduate Institute of Integrated Medicine, China Medical University
    Proteomics Core Laboratory, Department of Medical Research, China Medical University Hospital)

  • Yi-Fang Chiu

    (Institute of New Drug Development, China Medical University)

  • Yeh Chen

    (Institute of New Drug Development, China Medical University
    Research Center for Cancer Biology, China Medical University
    New Drug Development Center, China Medical University)

Abstract

Mammalian innate immune sensor STING (STimulator of INterferon Gene) was recently found to originate from bacteria. During phage infection, bacterial STING sense c-di-GMP generated by the CD-NTase (cGAS/DncV-like nucleotidyltransferase) encoded in the same operon and signal suicide commitment as a defense strategy that restricts phage propagation. However, the precise binding mode of c-di-GMP to bacterial STING and the specific recognition mechanism are still elusive. Here, we determine two complex crystal structures of bacterial STING/c-di-GMP, which provide a clear picture of how c-di-GMP is distinguished from other cyclic dinucleotides. The protein-protein interactions further reveal the driving force behind filament formation of bacterial STING. Finally, we group the bacterial STING into two classes based on the conserved motif in β-strand lid, which dictate their ligand specificity and oligomerization mechanism, and propose an evolution-based model that describes the transition from c-di-GMP-dependent signaling in bacteria to 2’3’-cGAMP-dependent signaling in eukaryotes.

Suggested Citation

  • Tzu-Ping Ko & Yu-Chuan Wang & Chia-Shin Yang & Mei-Hui Hou & Chao-Jung Chen & Yi-Fang Chiu & Yeh Chen, 2022. "Crystal structure and functional implication of bacterial STING," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-021-26583-3
    DOI: 10.1038/s41467-021-26583-3
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    References listed on IDEAS

    as
    1. Daniel Cohen & Sarah Melamed & Adi Millman & Gabriela Shulman & Yaara Oppenheimer-Shaanan & Assaf Kacen & Shany Doron & Gil Amitai & Rotem Sorek, 2019. "Cyclic GMP–AMP signalling protects bacteria against viral infection," Nature, Nature, vol. 574(7780), pages 691-695, October.
    2. Hannah G. Hampton & Bridget N. J. Watson & Peter C. Fineran, 2020. "The arms race between bacteria and their phage foes," Nature, Nature, vol. 577(7790), pages 327-336, January.
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    Cited by:

    1. Chia-Shin Yang & Tzu-Ping Ko & Chao-Jung Chen & Mei-Hui Hou & Yu-Chuan Wang & Yeh Chen, 2023. "Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Mei-Hui Hou & Yu-Chuan Wang & Chia-Shin Yang & Kuei-Fen Liao & Je-Wei Chang & Orion Shih & Yi-Qi Yeh & Manoj Kumar Sriramoju & Tzu-Wen Weng & U-Ser Jeng & Shang-Te Danny Hsu & Yeh Chen, 2023. "Structural insights into the regulation, ligand recognition, and oligomerization of bacterial STING," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Mei-Hui Hou & Chao-Jung Chen & Chia-Shin Yang & Yu-Chuan Wang & Yeh Chen, 2024. "Structural and functional characterization of cyclic pyrimidine-regulated anti-phage system," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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