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Published on: October 6, 2019
MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling
Jihuan Fu1, Yanbao Xiong, Youli Xu
1Key Laboratory of Infection and Immunity of Chinese Academy of Sciences, the Institute of Biophysics, 15 Da Tun Road, Chaoyang District, Beijing 100101, China.
Abstract:
Retinoic acid-inducible protein I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5) are cytosolic viral RNA sensors that induce type I interferon production (IFN). In this study, we found that MDA5 undergoes inducible SUMOylation by small ubiquitin-like modifier-1 (SUMO-1) in response to polyI:C stimulation. Enhanced SUMOylation of MDA5 by exogenously expressed SUMO-conjugating enzyme Ubc9 correlated with upregulation of IFN expression and repressed virus replication. Conversely, overexpression of a SUMOylation-deficient mutant of Ubc9 or knockdown of endogenous Ubc9 reduced IFN production. Furthermore, we showed that PIAS2β, a SUMOylation E3 ligase, could specifically interact with and enhance the SUMOylation of MDA5. Consequently, PIAS2β knockdown reduced the SUMOylation of MDA5 and the IFN production. Collectively, these findings suggest that SUMO-1 modification of MDA5 possibly via PIAS2β may play a role in the MDA5-mediated IFN response to viral infections.
Insights
Melanoma differentiation-associated gene 5 (MDA5) SUMOylation enhances interferon production against viral infections. This modification, involving SUMO-1 and Ubc9, is crucial for the innate immune response.
Area of Science:
- Immunology
- Molecular Biology
- Virology
Background:
- Retinoic acid-inducible protein I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5) are key cytosolic sensors of viral RNA.
- These sensors initiate the type I interferon (IFN) production, a critical component of the innate immune response against viral pathogens.
Purpose of the Study:
- To investigate the role of post-translational modifications, specifically SUMOylation, in MDA5-mediated antiviral signaling.
- To elucidate the molecular mechanisms by which MDA5 SUMOylation impacts IFN production and viral replication.
Main Methods:
- Stimulation of cells with polyI:C to mimic viral RNA presence.
- Analysis of MDA5 SUMOylation levels using specific antibodies.
- Overexpression and knockdown studies of SUMO-1, Ubc9, and PIAS2β.
- Measurement of IFN expression and viral replication rates.
Main Results:
- MDA5 undergoes inducible SUMOylation by SUMO-1 upon polyI:C stimulation.
- Enhanced MDA5 SUMOylation by Ubc9 correlated with increased IFN expression and reduced viral replication.
- PIAS2β, a SUMOylation E3 ligase, directly interacts with and enhances MDA5 SUMOylation.
- Knockdown of Ubc9 or PIAS2β impaired MDA5 SUMOylation and subsequent IFN production.
Conclusions:
- SUMO-1 modification of MDA5, potentially mediated by PIAS2β, plays a significant role in the MDA5-dependent IFN response to viral infections.
- This SUMOylation process is a critical regulatory mechanism in innate immunity against viruses.
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