Next Article in Journal
Influence of Herbicide Exposure and Ranavirus Infection on Growth and Survival of Juvenile Red-Eared Slider Turtles (Trachemys scripta elegans)
Next Article in Special Issue
Characterization of the SARS-CoV-2 Host Response in Primary Human Airway Epithelial Cells from Aged Individuals
Previous Article in Journal
Update in Diagnostics of Toscana Virus Infection in a Hyperendemic Region (Southern Spain)
Previous Article in Special Issue
Resveratrol and Pterostilbene Inhibit SARS-CoV-2 Replication in Air–Liquid Interface Cultured Human Primary Bronchial Epithelial Cells

SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity

Department of Medical Biotechnologies, University of Siena, 53100 Siena, Italy
“S. Maria delle Scotte” Hospital, Viale Bracci, 1, 53100 Siena, Italy
Author to whom correspondence should be addressed.
Academic Editors: Concetta Castilletti, Luisa Barzon and Francesca Colavita
Viruses 2021, 13(8), 1439;
Received: 22 June 2021 / Revised: 19 July 2021 / Accepted: 22 July 2021 / Published: 23 July 2021
(This article belongs to the Special Issue SARS-CoV-2 Host Cell Interactions)
A weak production of INF-β along with an exacerbated release of pro-inflammatory cytokines have been reported during infection by the novel SARS-CoV-2 virus. SARS-CoV-2 encodes several proteins able to counteract the host immune system, which is believed to be one of the most important features contributing to the viral pathogenesis and development of a severe clinical picture. Previous reports have demonstrated that SARS-CoV-2 N protein, along with some non-structural and accessory proteins, efficiently suppresses INF-β production by interacting with RIG-I, an important pattern recognition receptor (PRR) involved in the recognition of pathogen-derived molecules. In the present study, we better characterized the mechanism by which the SARS-CoV-2 N counteracts INF-β secretion and affects RIG-I signaling pathways. In detail, when the N protein was ectopically expressed, we noted a marked decrease in TRIM25-mediated RIG-I activation. The capability of the N protein to bind to, and probably mask, TRIM25 could be the consequence of its antagonistic activity. Furthermore, this interaction occurred at the SPRY domain of TRIM25, harboring the RNA-binding activity necessary for TRIM25 self-activation. Here, we describe new findings regarding the interplay between SARS-CoV-2 and the IFN system, filling some gaps for a better understanding of the molecular mechanisms affecting the innate immune response in COVID-19. View Full-Text
Keywords: innate immunity; SARS-CoV-2 N protein; RIG-I activation innate immunity; SARS-CoV-2 N protein; RIG-I activation
Show Figures

Figure 1

MDPI and ACS Style

Gori Savellini, G.; Anichini, G.; Gandolfo, C.; Cusi, M.G. SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity. Viruses 2021, 13, 1439.

AMA Style

Gori Savellini G, Anichini G, Gandolfo C, Cusi MG. SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity. Viruses. 2021; 13(8):1439.

Chicago/Turabian Style

Gori Savellini, Gianni, Gabriele Anichini, Claudia Gandolfo, and Maria G. Cusi. 2021. "SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity" Viruses 13, no. 8: 1439.

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

Back to TopTop