Back to Search
Start Over
The Interaction between SARS-CoV-2 Nucleocapsid Protein and UBC9 Inhibits MAVS Ubiquitination by Enhancing Its SUMOylation.
- Source :
-
Viruses (1999-4915) . Dec2023, Vol. 15 Issue 12, p2304. 15p. - Publication Year :
- 2023
-
Abstract
- Severe COVID-19 patients exhibit impaired IFN-I response due to decreased IFN-β production, allowing persistent viral load and exacerbated inflammation. While the SARS-CoV-2 nucleocapsid (N) protein has been implicated in inhibiting innate immunity by interfering with IFN-β signaling, the specific underlying mechanism still needs further investigation for a comprehensive understanding. This study reveals that the SARS-CoV-2 N protein enhances interaction between the human SUMO-conjugating enzyme UBC9 and MAVS. Increased MAVS-UBC9 interaction leads to enhanced SUMOylation of MAVS, inhibiting its ubiquitination, resulting in the inhibition of phosphorylation events involving IKKα, TBK1, and IRF3, thus disrupting IFN-β signaling. This study highlights the role of the N protein of SARS-CoV-2 in modulating the innate immune response by affecting the MAVS SUMOylation and ubiquitination processes, leading to inhibition of the IFN-β signaling pathway. These findings shed light on the complex mechanisms utilized by SARS-CoV-2 to manipulate the host's antiviral defenses and provide potential insights for developing targeted therapeutic strategies against severe COVID-19. [ABSTRACT FROM AUTHOR]
- Subjects :
- *UBIQUITINATION
*SARS-CoV-2
*COVID-19
*VIRAL load
*PROTEINS
Subjects
Details
- Language :
- English
- ISSN :
- 19994915
- Volume :
- 15
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Viruses (1999-4915)
- Publication Type :
- Academic Journal
- Accession number :
- 174493540
- Full Text :
- https://doi.org/10.3390/v15122304