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血红素加氧酶-1对I型干扰素信号传导的双向调节

Bi-directional regulation of type I interferon signaling by heme oxygenase-1.

作者信息

Wu Miaomiao, Fan Yihui, Li Lijuan, Yuan Junfa

机构信息

Department of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.

Hubei Engineering Research Center for Aquatic Animal Diseases Control and Prevention, Wuhan 430070, People's Republic of China.

出版信息

iScience. 2024 Feb 8;27(3):109185. doi: 10.1016/j.isci.2024.109185. eCollection 2024 Mar 15.

DOI:10.1016/j.isci.2024.109185
PMID:38420586
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10901085/
Abstract

Moderate activation of IFN-I contributes to the body's immune response, but its abnormal expression, stimulated by oxidative stress or other factors causes pathological damage. Heme oxygenase-1 (HO-1), induced by stress stimuli in the body, exerts a central role in cellular protection. Here we showed that HO-1 could promote IFN-1 under Spring Viremia of Carp virus (SVCV) infection and concomitantly attenuate the replication of SVCV. Further characterization of truncated mutants of HO-1 confirmed that intact HO-1 was essential for its antiviral function via IFN-I. Importantly, HO-1 inhibited the IFN-I signal by degrading the IRF3/7 through the autophagy pathway when it was triggered by HO treatment. The iron ion-binding site (His28) was critical for HO-1 to degrade IRF3/7. HO-1 degradation of IRF3/7 is conserved in fish and mammals. Collectively, HO-1 regulates IFN-I positively under viral infection and negatively under oxidative stress, elucidating a mechanism by which HO-1 regulates IFN-I signaling in bi-directions.

摘要

I型干扰素的适度激活有助于机体的免疫反应，但其受氧化应激或其他因素刺激而异常表达会导致病理损伤。血红素加氧酶-1（HO-1）由机体应激刺激诱导产生，在细胞保护中发挥核心作用。在此我们表明，HO-1在鲤春病毒血症病毒（SVCV）感染时可促进I型干扰素的产生，并同时减弱SVCV的复制。对HO-1截短突变体的进一步表征证实，完整的HO-1通过I型干扰素对其抗病毒功能至关重要。重要的是，当HO处理触发自噬途径时，HO-1通过降解IRF3/7来抑制I型干扰素信号。铁离子结合位点（His28）对HO-1降解IRF3/7至关重要。HO-1对IRF3/7的降解在鱼类和哺乳动物中是保守的。总体而言，HO-1在病毒感染时正向调节I型干扰素，在氧化应激时负向调节，阐明了HO-1双向调节I型干扰素信号的机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/278ce2f72791/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/0afb39842616/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/5150e5cdbada/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/bbabbe72fc42/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/2bf784bacb51/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/9d24bbac55e6/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/9264528a940f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/d1f03d76bcf2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/5a5bd2995d9f/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/278ce2f72791/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/0afb39842616/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/5150e5cdbada/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/bbabbe72fc42/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/2bf784bacb51/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/9d24bbac55e6/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/9264528a940f/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/d1f03d76bcf2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/5a5bd2995d9f/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97e0/10901085/278ce2f72791/gr8.jpg

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