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- W4310477279 abstract "The mediator of IRF3 activation (MITA, also named STING) is critical for immune responses to abnormal cytosolic DNA and has been considered an important drug target in the clinical therapy of tumors and autoimmune diseases. In the present study, we report that MITA undergoes DDOST-mediated N-glycosylation in the endoplasmic reticulum (ER) upon DNA viral infection. Selective mutation of DDOST-dependent N-glycosylated residues abolished MITA oligomerization and thereby its immune functions. Moreover, increasing the expression of Ddost in the mouse brain effectively strengthens the local immune response to herpes simplex virus-1 (HSV-1) and prolongs the survival time of mice with HSV encephalitis (HSE). Our findings reveal the dependence of N-glycosylation on MITA activation and provide a new perspective on the pathogenesis of HSE." @default.
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- W4310477279 date "2022-11-30" @default.
- W4310477279 modified "2023-10-15" @default.
- W4310477279 title "MITA oligomerization upon viral infection is dependent on its N-glycosylation mediated by DDOST" @default.
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- W4310477279 doi "https://doi.org/10.1371/journal.ppat.1010989" @default.
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