Evidence map›Paper›PMID 35013136›Full record

ArticleNature communications2022

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, Yeh Chen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 35 citations in OpenAlex.

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  17. The Many Ways to Deal with STING.International journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Tzu-Ping Ko *Institute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan.ORCID 0000-0003-1794-2638
Yu-Chuan Wang *Institute of New Drug Development, China Medical University, Taichung, 406, Taiwan.
Chia-Shin Yang *Institute of New Drug Development, China Medical University, Taichung, 406, Taiwan.
Mei-Hui Hou *Institute of New Drug Development, China Medical University, Taichung, 406, Taiwan.
Chao-Jung ChenGraduate Institute of Integrated Medicine, China Medical University, Taichung, 406, Taiwan.ORCID 0000-0003-3834-9243
Yi-Fang ChiuInstitute of New Drug Development, China Medical University, Taichung, 406, Taiwan.
Yeh ChenInstitute of New Drug Development, China Medical University, Taichung, 406, Taiwan. chyeah6599@mail.cmu.edu.tw.ORCID 0000-0002-7740-0446
China Medical University · TWInstitute of Biological Chemistry, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Immunity, InnateBacteriaCrystallography, X-RayCyclic GMPCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseDinucleoside PhosphatesHumansInterferonsLigandsMembrane ProteinsNucleotidyltransferasesPrevotellaSTING Proteinbis(3',5')-cyclic diguanylic acidcGAS protein, humanCyclic GMPCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseDinucleoside PhosphatesInterferonsLigandsMembrane ProteinsNucleotidyltransferasesSTING1 protein, humanSTING Protein

Identifiers

PMID35013136
PMCPMC8748872
OpenAlexW4206234635

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.