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Oxygen enhances antiviral innate immunity through maintenance of EGLN1-catalysed proline hydroxylation of IRF3

ABSTRACT: Oxygen enhances antiviral innate immunity through maintenance of EGLN1-catalysed proline hydroxylation of IRF3

PROVIDER: PRJNA1064164 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27513336_1.fastq.gz	Fastqsanger.gz
	SRR27513336_2.fastq.gz	Fastqsanger.gz
	SRR27513338_1.fastq.gz	Fastqsanger.gz
	SRR27513338_2.fastq.gz	Fastqsanger.gz
	SRR27513340_1.fastq.gz	Fastqsanger.gz

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Oxygen enhances antiviral innate immunity through maintenance of EGLN1-catalysed proline hydroxylation of IRF3

Project description:Oxygen is essential for aerobic organisms, but little is known about its role in antiviral immunity. Here, we report that during responses to viral infection, the hypoxic conditions repress antiviral-responsive genes independently of HIF signalling. EGLN1 was identified as a key mediator of the enhancement exerted by the oxygen on antiviral innate immune responses. Under sufficient oxygen conditions, EGLN1 maintains its prolyl hydroxylase activity to catalyse hydroxylation of IRF3 at proline 10. This modification enhances IRF3 phosphorylation, dimerisation, and nuclear translocation, leading to subsequent IRF3 activation. Furthermore, mice and zebrafish with Egln1 deletion, treatment with the EGLN inhibitor, FG4592, or mice carrying an Irf3 P10A mutation are more susceptible to viral infections. These findings not only reveal a direct link between oxygen and antiviral responses, but also provide insights into the mechanisms by which oxygen regulates innate immunity

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Proline hydroxylation of ChREBP

Project description:This project investigated proline hydroxylation of ChREBP. Proline hydroxylation was investigated in flag-IP enriched protein extracts from ChREBP-flag overexpressing HEK293 cells (A) and in ChREBP-IP enriched mouse liver protein (male, C57BL6/J) (B).

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Project description:Histone H3 proline 16 hydroxylation regulates mammalian gene expression

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AXIN1 boosts antiviral response through IRF3 stabilization and induced phase separation

Project description:Axis inhibition protein 1 (AXIN), a scaffold protein interacting with various critical molecules, plays a vital role in determining cell fate. However, its impact on the antiviral innate immune response remains largely unknown. Here, we identify AXIN acts as an effective regulator of antiviral innate immunity against both DNA and RNA virus infections. In the resting state, AXIN maintains the stability of IRF3 by preventing p62-mediated autophagic degradation of IRF3. This is achieved by recruiting ubiquitin-specific peptidase 35 (USP35), which removes lysine (K) 48-linked ubiquitination at IRF3 K366. Upon virus infection, AXIN undergoes a phase separation triggered by phosphorylated TBK1. This leads to increased phosphorylation of IRF3 and a boost in IFN-I production. Moreover, KYA1797K, a small molecule that binds to the AXIN RGS domain, enhances the AXIN-IRF3 interaction and promotes the elimination of various highly pathogenic viruses. Clinically, patients with HBV-associated hepatocellular carcinoma (HCC) who show reduced AXIN expression in pericarcinoma tissues have low overall and disease-free survival rates, as well as higher HBV levels in their blood. Overall, our findings reveal how AXIN regulates IRF3 signaling and phase separation-mediated antiviral immune responses, underscoring the potential of the AXIN agonist KYA1797K as an effective antiviral agent.

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Histone H3 proline 16 hydroxylation regulates mammalian gene expression [RNA-Seq]

Project description:Histone posttranslational modifications (PTMs) are important for regulating various DNA-templated processes. Emerging evidence suggests a critical involvement of the previously less-explored histone PTMs in gene activity regulation. Here, we report the existence of a new histone PTM in the mammalian cells, hydroxylation of H3 proline 16 (H3P16-OH) catalyzed by EglN2, a proline hydroxylase. We show that EglN2-mediated H3P16-OH enhances direct binding of Lysine-Specific Demethylase 5A (KDM5A) with its substrate, H3 lysine 4 trimethylation (H3K4me3), resulting in enhanced chromatin recruitment of KDM5A and decrease of H3K4me3 at target genes. Genome-wide mapping by CUT&RUN in multiple mammalian cell models reveals a functional connection between EglN2, H3P16-OH, KDM5A and H3K4me3. Integrated analysis with RNA-Seq also identifies distinct subsets of genes that are regulated through H3P16-OH in different cell lines. This study therefore demonstrates a new player of the “histone code” by revealing a role of H3P16-OH in regulating gene expression in mammalian cells.

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