Evidence map›Paper›PMID 39524340›Full record

ArticleiScience2024

Porcine NLRC3 specially binds short dsDNA to regulate cGAS activation.

Minjie Li, Cheng Zhu, Ye Yuan, Xiangyu Huang, Lei Wu, Jiayang Wu, Hongyan Yin, Lvye Chai, Weiyu Qu, Ya Yan and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

12 authors.

Minjie LiNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Cheng ZhuTianjin Key Laboratory of Function and Application of Biological Macromolecular Structures, School of Life Sciences, Tianjin University, Tianjin 300072, China.
Ye YuanNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Xiangyu HuangNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Lei WuNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Jiayang WuTianjin Key Laboratory of Function and Application of Biological Macromolecular Structures, School of Life Sciences, Tianjin University, Tianjin 300072, China.
Hongyan YinNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Lvye ChaiNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Weiyu QuNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Ya YanNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.
Pingwei LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Xin LiNational Key Laboratory of Veterinary Public Health and Safety, China Agricultural University, Beijing 100193, China.

Funding

Molecular basis of viral DNA sensing through the cGAS-STING pathwayR01AI145287 · NIAID · TEXAS A&M AGRILIFE RESEARCH · PI Pingwei Li · 2019 to 2026
$2.5M
NIAID NIH HHS R01 AI145287
6 · The paper itself

Abstract

Host immune system has evolved multiple sensors to detect pathogenic and damaged DNA, where precise regulation is critical for distinguishing self from non-self. Our previous studies showed that NLRC3 is an inhibitory nucleic acid sensor that binds to viral DNA and thereby unleashing STING activation. In this study, we demonstrate that human NLRC3 favors long dsDNA, while porcine NLRC3 shows an affinity for shorter dsDNA. Mechanistically, a conserved arginine residue within the leucine-rich repeats of primates NLRC3 forms a structural bridge facilitating the binding of long dsDNA. Conversely, a glycine residue that replaces the arginine in non-primates disrupts this bridge. Furthermore, porcine NLRC3 negatively regulates type I interferon by interacting with cyclic GMP-AMP synthase (cGAS) to inhibit its DNA binding, thereby preventing cGAS activation. These results reveal an unrecognized mechanism by which a species-specific amino acid variation of NLRC3 influences nucleic acid recognition, providing insights into the evolution of innate immunity to pathogens.

Indexed as

Immune responseImmunologyMolecular biology

Identifiers

PMID39524340
PMCPMC11544074

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.