PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses

Abstract VISA/MAVS is crucial in antiviral innate immunity. Upon RNA virus infection, VISA recruits TBK1 via TRAFs to mitochondria, inducing IRF3 phosphorylation and type I interferons. However, TBK1 recruitment mechanisms via individual TRAFs are unclear. Here, we reveal that PWWP domain-containing...

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Main Authors: Mengling Shi, Cong Wang, Zhen Chen, Yidan Zhou, Liang Yue, Yu Liu, Tiannan Guo, Jun Shang, Haotian Xu, Yu Zhang, Mengcheng Luo, Caoqi Lei
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-59421-x
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author Mengling Shi
Cong Wang
Zhen Chen
Yidan Zhou
Liang Yue
Yu Liu
Tiannan Guo
Jun Shang
Haotian Xu
Yu Zhang
Mengcheng Luo
Caoqi Lei
author_facet Mengling Shi
Cong Wang
Zhen Chen
Yidan Zhou
Liang Yue
Yu Liu
Tiannan Guo
Jun Shang
Haotian Xu
Yu Zhang
Mengcheng Luo
Caoqi Lei
author_sort Mengling Shi
collection DOAJ
description Abstract VISA/MAVS is crucial in antiviral innate immunity. Upon RNA virus infection, VISA recruits TBK1 via TRAFs to mitochondria, inducing IRF3 phosphorylation and type I interferons. However, TBK1 recruitment mechanisms via individual TRAFs are unclear. Here, we reveal that PWWP domain-containing 3A (PWWP3A) serves as a negative regulator of RNA virus-triggered signaling. During viral infection, PWWP3A translocates from nucleus to the mitochondria, competing with TRAF6 for binding to VISA, thereby impeding the recruitment of TBK1 and inhibiting IRF3 activation. However, the extent of PWWP3A-mediated inhibition is regulated by the E3 ligase PJA2, which induces PWWP3A degradation post-infection, highlighting the intricate regulatory network in antiviral immunity. Consistently, PWWP3A deficiency enhances antiviral responses, and Pwwp3a −/− mice exhibit elevated levels of type I interferons and displayed greater resistance following RNA virus infection. Together, our findings unveil the inhibitory role of PWWP3A in virus-triggered signaling, which provides insights into preventing excessive immune responses.
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spelling doaj-art-7f5f8371e7ff4c8fbc089925788b6c2a2025-08-20T01:47:29ZengNature PortfolioNature Communications2041-17232025-05-0116111510.1038/s41467-025-59421-xPWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA virusesMengling Shi0Cong Wang1Zhen Chen2Yidan Zhou3Liang Yue4Yu Liu5Tiannan Guo6Jun Shang7Haotian Xu8Yu Zhang9Mengcheng Luo10Caoqi Lei11State Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversityState Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversityState Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversityDepartment of Epidemiology and Biostatistics, School of Public Health, Wuhan University, Wuhan UniversityCenter for Intelligent Proteomics, Westlake Laboratory of Life Sciences and BiomedicineState Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversityCenter for Intelligent Proteomics, Westlake Laboratory of Life Sciences and BiomedicineSpecAlly Life Technology Co. Ltd.State Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversitySchool of Basic Medical Sciences, Lanzhou UniversityHubei Provincial Key Laboratory of Developmentally Originated Disease, TaiKang Center for Life and Medical Sciences, School of Basic Medical Sciences, Wuhan UniversityState Key Laboratory of Virology and Biosafety, College of Life Sciences, Frontier Science Center for Immunology and Metabolism, Wuhan UniversityAbstract VISA/MAVS is crucial in antiviral innate immunity. Upon RNA virus infection, VISA recruits TBK1 via TRAFs to mitochondria, inducing IRF3 phosphorylation and type I interferons. However, TBK1 recruitment mechanisms via individual TRAFs are unclear. Here, we reveal that PWWP domain-containing 3A (PWWP3A) serves as a negative regulator of RNA virus-triggered signaling. During viral infection, PWWP3A translocates from nucleus to the mitochondria, competing with TRAF6 for binding to VISA, thereby impeding the recruitment of TBK1 and inhibiting IRF3 activation. However, the extent of PWWP3A-mediated inhibition is regulated by the E3 ligase PJA2, which induces PWWP3A degradation post-infection, highlighting the intricate regulatory network in antiviral immunity. Consistently, PWWP3A deficiency enhances antiviral responses, and Pwwp3a −/− mice exhibit elevated levels of type I interferons and displayed greater resistance following RNA virus infection. Together, our findings unveil the inhibitory role of PWWP3A in virus-triggered signaling, which provides insights into preventing excessive immune responses.https://doi.org/10.1038/s41467-025-59421-x
spellingShingle Mengling Shi
Cong Wang
Zhen Chen
Yidan Zhou
Liang Yue
Yu Liu
Tiannan Guo
Jun Shang
Haotian Xu
Yu Zhang
Mengcheng Luo
Caoqi Lei
PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
Nature Communications
title PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
title_full PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
title_fullStr PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
title_full_unstemmed PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
title_short PWWP3A disrupts the assembly of VISA/MAVS signalosome to inhibit innate immune response against RNA viruses
title_sort pwwp3a disrupts the assembly of visa mavs signalosome to inhibit innate immune response against rna viruses
url https://doi.org/10.1038/s41467-025-59421-x
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