Cited by 590SARS-CoV-2 and COVID-19 ResearchRNA Research and Splicinginterferon and immune responses

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SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

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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, Thai, Jasmine, 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·2020·Cell

DOI 10.1016/j.cell.2020.10.004PMC PMC7543886

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Abstract

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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Bolger, A. M., Lohse, M., & Usadel, B. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu170 · Cited by 65,548
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
The Protein Data Bank
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Integrative genomics viewer
Robinson, J. T., Thorvaldsdóttir, H., Winckler, W., Guttman, M., Lander, E. S., Getz, G., & Mesirov, J. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1754 · Cited by 15,390
Self-citation
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807
Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
Alexopoulou, L., Holt, A. C., Medzhitov, R., & Flavell, R. A. (2001) · Nature · doi:10.1038/35099560 · Cited by 6,129
The proximal origin of SARS-CoV-2
Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081
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Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s15 · Cited by 4,618

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FAIRsharing record for: scMOVIR
FAIRsharing Team, et al. (2026) · FAIRsharing.org · doi:10.25504/fairsharing.3e1f6e

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)
DOI: 10.1016/j.cell.2020.10.004
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
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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SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses

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