SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses
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Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a recently identified coronavirus that causes the respiratory disease known as coronavirus disease 2019 (COVID-19). Despite the urgent need, we still do not fully understand the molecular basis of SARS-CoV-2 pathogenesis. Here, we comprehensively define the interactions between SARS-CoV-2 proteins and human RNAs. NSP16 binds to the mRNA recognition domains of the U1 and U2 splicing RNAs and acts to suppress global mRNA splicing upon SARS-CoV-2 infection. NSP1 binds to 18S ribosomal RNA in the mRNA entry channel of the ribosome and leads to global inhibition of mRNA translation upon infection. Finally, NSP8 and NSP9 bind to the 7SL RNA in the signal recognition particle and interfere with protein trafficking to the cell membrane upon infection. Disruption of each of these essential cellular functions acts to suppress the interferon response to viral infection. Our results uncover a multipronged strategy utilized by SARS-CoV-2 to antagonize essential cellular processes to suppress host defenses.
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A main evasion strategy seems to be blocking type I interferon responses at several steps, such as viral RNA recognition, nuclear translocation of inflammatory transcription factors, and STAT1/STAT2 phosphorylation.
“A predominant strategy appears to be the inhibition of the type I interferon response58–60 at multiple points, including impaired recognition of viral RNA61,62, decreased nuclear translocation of pro-inflammatory transcription factors (such as IRF3, IRF7 and STAT1)61,63 and suppression of STAT1 and STAT2 phosphorylation64,65.”
From Immunological mechanisms of vaccine-induced protection against COVID-19 in humans (2021) · cites this paper as [61]
NSP16 suppresses global mRNA splicing and diminishes recognition of viral RNA by intracellular helicase receptors; NSP1 inhibits mRNA translation by binding 18S ribosomal RNA; NSP8 and NSP9 interfere with protein trafficking to the cell membrane; all three mechanisms independently reduce type I IFN production.
“SARS-CoV-2-derived non-structural protein 16 (NSP16) suppresses global mRNA splicing and diminishes recognition of viral RNA by intracellular helicase receptors, NSP1 leads to global inhibition of mRNA translation by binding to the 18S ribosomal RNA in the mRNA entry channel, and NSP8 and NSP9 interfere with protein trafficking to the cell membrane; all three mechanisms independently leading to”
From COVID-19 and the human innate immune system (2021) · cites this paper as Banerjee et al., 2020
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Interferon induction, evasion, and paradoxical roles during SARS‐CoV‐2 infection*
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Delivery Routes for COVID-19 Vaccines
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SARS-CoV-2 Nsp14 mediates the effects of viral infection on the host cell transcriptome
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Characterization of SARS-CoV-2 Evasion: Interferon Pathway and Therapeutic Options
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- Authors
- Banerjee, A. K., Blanco, M. R., Bruce, E. A., Honson, D. D., Chen, L. M., Chow, A., Bhat, P., Ollikainen, N., Quinodoz, S. A., Loney, C., Thai, J., Miller, Z. D., Lin, A. E., Schmidt, M. M., Stewart, D. G., Goldfarb, D., De Lorenzo, G., Rihn, S. J., Voorhees, R. M., Botten, J. W., Majumdar, D., & Guttman, M.
- Affiliations
- University of Southern California (US)
- California Institute of Technology (US)
- University of Vermont (US)
- MRC University of Glasgow Centre for Virus Research (GB)
- Broad Institute (US)
- Corresponding author
- Majumdar, Devdoot
- Guttman, Mitchell
- ORCID
- Banerjee, Abhik K.
- Blanco, Mario R.
- Bruce, Emily A.
- Honson, Drew D.
- Chen, Linlin M.
- Chow, Amy
- Bhat, Prashant
- Ollikainen, Noah
- Quinodoz, Sofia A.
- Loney, Colin
- Miller, Zachary D.
- Lin, Aaron E.
- Schmidt, Madaline M.
- Stewart, Douglas G.
- Goldfarb, Daniel
- De Lorenzo, Giuditta
- Rihn, Suzannah J.
- Voorhees, Rebecca M.
- Botten, Jason W.
- Majumdar, Devdoot
- Guttman, Mitchell
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-11
- Volume
- 183
- Issue
- 5
- Pages
- 1325-1339.e21
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7543886
- OpenAlex
- W3092296275
- Cited by
- 583
- References
- 100
- Citations by year
- 2026: 40 · 2025: 64 · 2024: 80 · 2023: 106 · 2022: 149 · 2021: 129 · 2020: 15
- FWCI
- 13.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by)
- Funders
- Wellcome Trust
- University of Vermont
- Heritage Medical Research Institute
- American Cancer Society
- Foundation for the National Institutes of Health
- Chan Zuckerberg Initiative
- California Institute of Technology
- New York Stem Cell Foundation
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- SARS-CoV-2, COVID-19 pandemic, host-virus interaction, nsp16, Nsp1, 18S rRNA, mRNA translation inhibition, nsp8, nsp9, 7SL RNA, signal recognition particle, protein trafficking, viral pathogenesis
- MeSH terms
- A549 Cells, COVID-19, SARS-CoV-2, Animals, Chlorocebus aethiops, Humans, Interferons, RNA Splicing, RNA, Messenger, RNA, Ribosomal, 18S, Protein Biosynthesis, Vero Cells, Viral Nonstructural Proteins, Signal Recognition Particle, RNA, Small Cytoplasmic, Protein Transport, Host-Pathogen Interactions, HEK293 Cells
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