Human cytomegalovirus IE86 protein aa 136-289 mediates STING degradation and blocks the cGAS-STING pathway
- Authors
- Lee, Jun-Kyu; Kim, Jung-Eun; Park, Bang Ju; Song, Yoon-Jae
- Issue Date
- Jan-2020
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- HCMV; IE86; STING; type I IFN
- Citation
- JOURNAL OF MICROBIOLOGY, v.58, no.1, pp.54 - 60
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 58
- Number
- 1
- Start Page
- 54
- End Page
- 60
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/26185
- DOI
- 10.1007/s12275-020-9577-6
- ISSN
- 1225-8873
- Abstract
- We previously reported that human cytomegalovirus (HCMV) 86 kDa immediate-early 2 gene product (IE86) promotes proteasome-dependent degradation of STING. In the present study, we determined the specific residues of IE86 responsible for STING degradation using a STING-firefly luciferase fusion protein expression system for quantitative meas-urement of STING protein levels. IE86 amino acids (aa) 136-289 were sufficient to promote STING degradation and further induced down-regulation of 2 ' 3 '-cyclic GMP-AMP (cGAMP)-mediated IFN-beta promoter activation. Interestingly, transactivation domains (TAD) of the IE86 protein located at the N- and C-termini were required for down-regulation of Toll/interleukin-1 receptor (TIR) domain-containing adaptor-inducing interferon beta (IFN-beta) (TRIF)-mediated IFN-beta-and p65/RelA-induced NF-kappa B-dependent promoter activation while amino acids (aa) 136-289 had no significant effects. Our collective data suggest that the IE86 protein utilizes the aa 136-289 region to promote STING degradation and inhibit the cGAS-STING pathway.
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