Crystal structure and functional implication of bacterial STING

Tzu-Ping Ko, Yu-Chuan Wang, Chia-Shin Yang, Mei-Hui Hou, Chao-Jung Chen, Yi-Fang Chiu and Yeh Chen ()
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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
Yi-Fang Chiu: Institute of New Drug Development, China Medical University
Yeh Chen: Institute of New Drug Development, China Medical University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-021-26583-3

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