USP13 negatively regulates antiviral responses by deubiquitinating STING

He Sun, Qiang Zhang, Ying-Ying Jing, Man Zhang, Hai-Ying Wang, Zeng Cai, Tianzi Liuyu, Zhi-Dong Zhang, Tian-Chen Xiong, Yan Wu, Qi-Yun Zhu, Jing Yao, Hong-Bing Shu, Dandan Lin and Bo Zhong ()
Additional contact information
He Sun: College of Life Sciences, Wuhan University
Qiang Zhang: College of Life Sciences, Wuhan University
Ying-Ying Jing: College of Life Sciences, Wuhan University
Man Zhang: College of Life Sciences, Wuhan University
Hai-Ying Wang: College of Life Sciences, Wuhan University
Zeng Cai: College of Life Sciences, Wuhan University
Tianzi Liuyu: College of Life Sciences, Wuhan University
Zhi-Dong Zhang: Medical Research Institute, School of Medicine, Wuhan University
Tian-Chen Xiong: Medical Research Institute, School of Medicine, Wuhan University
Yan Wu: National Institute of Biological Sciences
Qi-Yun Zhu: State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences
Jing Yao: College of Life Sciences, Wuhan University
Hong-Bing Shu: Medical Research Institute, School of Medicine, Wuhan University
Dandan Lin: Cancer Center, Renmin Hospital of Wuhan University
Bo Zhong: College of Life Sciences, Wuhan University

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: Abstract STING (also known as MITA) is critical for host defence against viruses and the activity of STING is regulated by ubiquitination. However, the deubiquitination of STING is not fully understood. Here, we show that ubiquitin-specific protease 13 (USP13) is a STING-interacting protein that catalyses deubiquitination of STING. Knockdown or knockout of USP13 potentiates activation of IRF3 and NF-κB and expression of downstream genes after HSV-1 infection or transfection of DNA ligands. USP13 deficiency results in impaired replication of HSV-1. Consistently, USP13 deficient mice are more resistant than wild-type littermates to lethal HSV-1 infection. Mechanistically, USP13 deconjugates polyubiquitin chains from STING and prevents the recruitment of TBK1 to the signalling complex, thereby negatively regulating cellular antiviral responses. Our study thus uncovers a function of USP13 in innate antiviral immunity and provides insight into the regulation of innate immunity.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms15534 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15534

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms15534

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().