Human Cytomegalovirus IE2 86 kDa Protein Induces STING Degradation and Inhibits cGAMP- Mediated IFN-beta Induction
- Authors
- Kim, Jung-Eun; Kim, Young-Eui; Stinski, Mark F.; Ahn, Jin-Hyun; Song, Yoon-Jae
- Issue Date
- 26-Sep-2017
- Publisher
- FRONTIERS MEDIA SA
- Keywords
- HCMV; IE86; STING; IFN; cGAMP
- Citation
- FRONTIERS IN MICROBIOLOGY, v.8
- Journal Title
- FRONTIERS IN MICROBIOLOGY
- Volume
- 8
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/5695
- DOI
- 10.3389/fmicb.2017.01854
- ISSN
- 1664-302X
- Abstract
- Stimulator of interferon genes (STING) is a critical signaling molecule in the innate immune response against DNA viruses by either directly sensing intracellular DNA or functioning as an adaptor molecule to activate the type I interferon (IFN) signaling pathway. We determined the functional interaction between STING and human cytomegalovirus (HCMV). A cDNA library containing 133 HCMV ORFs was screened to identify viral genes that inhibit STING-induced IFN-beta promoter activation. Among the screened ORFs, UL122, which encodes the immediate-early 2 86 kDa (IE86) protein, strongly abolished STING-induced IFN-b promoter activation. Interestingly, IE86 protein facilitated the proteasome-dependent degradation of STING and inhibited 2'3' -cGAMPmediated induction of IFNB1 and CXCL10. Taken together, this study demonstrates the existence of a post-translational regulation of STING by HCMV IE86 protein.
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