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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 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]
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“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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Cites
Trimmomatic: a flexible trimmer for Illumina sequence data
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
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
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-citationThe 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
Comparative Protein Structure Modeling Using Modeller
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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SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874
The trRosetta server for fast and accurate protein structure prediction
Du, Z., Su, H. L., Wang, W., Ye, L., Wei, H., Peng, Z., Anishchenko, I. V., Baker, D. A., & Yang, J. (2021) · Nature Protocols · doi:10.1038/s41596-021-00628-9 · Cited by 737
COVID-19 and the human innate immune system
Schultze, J. L., & Aschenbrenner, A. C. (2021) · Cell · doi:10.1016/j.cell.2021.02.029 · Cited by 714
“…translation by binding to the 18S ribosomal RNA in themRNA entry channel, and NSP8 and NSP9 interfere with protein trafficking to the cell membrane; all three mechanisms independently leading to reduction of type I IFN production by the affected cell (Banerjee et al., 2020; Gordon et al., 2020).”
BackgroundImmunological mechanisms of vaccine-induced protection against COVID-19 in humans
Sadarangani, M., Marchant, A., & Kollmann, T. R. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00578-z · Cited by 560
Malone, B. F., Urakova, N., Snijder, E. J., & Campbell, E. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00432-z · Cited by 583
Regulation of RIG-I-like receptor-mediated signaling: interaction between host and viral factors
Onomoto, K., Onoguchi, K., & Yoneyama, M. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-00602-7 · Cited by 440
CLIP and complementary methods
Hafner, M., Katsantoni, M., Köster, T., Marks, J., Mukherjee, J., Staiger, D., Ule, J., & Zavolan, M. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00018-1 · Cited by 406
Khan, M., Yoo, S., Clijsters, M., Backaert, W., Vanstapel, A., Speleman, K., Lietaer, C., Choi, S., HETHER, T. D., Marcelis, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.10.027 · Cited by 393
Human genetic and immunological determinants of critical COVID-19 pneumonia
Zhang, Q., Bastard, P., Effort, C. H. G., Karbuz, A., Gervais, A., Tayoun, A. N. A., Aiuti, A., Bélot, A., Bolze, A., Gaudet, A., et al. (2022) · Nature · doi:10.1038/s41586-022-04447-0 · Cited by 377
Impaired local intrinsic immunity to SARS-CoV-2 infection in severe COVID-19
Ziegler, C. G. K., Miao, V. N., Owings, A. H., Navia, A. W., Tang, Y., Bromley, J. D., Lotfy, P., Sloan, M., Laird, H., Williams, H. B., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.023 · Cited by 358
The SARS-CoV-2 RNA–protein interactome in infected human cells
Schmidt, N., Lareau, C. A., Keshishian, H., Ganskih, S., Schneider, C., Hennig, T., Melanson, R., Werner, S., Wei, Y., Zimmer, M., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00846-z · Cited by 319
Ribosome biogenesis in disease: new players and therapeutic targets
Jiao, L., Liu, Y., Yu, X., Pan, X., Zhang, Y., Tu, J., Song, Y., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01285-4 · Cited by 336
Type I and III interferon responses in SARS-CoV-2 infection
Kim, Y., & Shin, E. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00592-0 · Cited by 304
Lam, S. M., Zhang, C., Wang, Z., Zhen, N., Zhang, S., Yang, S., Huang, X., Mo, L., Li, J., Lee, B. T. K., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00425-4 · Cited by 285
SARS-CoV-2-Specific Immune Response and the Pathogenesis of COVID-19
Gusev, E., Sarapultsev, A., Владимировна, С. Л., & Черешнев, В. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031716 · Cited by 326
The interferon landscape along the respiratory tract impacts the severity of COVID-19
Sposito, B., Broggi, A., Pandolfi, L., Crotta, S., Clementi, N., Ferrarese, R., Sisti, S., Criscuolo, E., Spreafico, R., Long, J. M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.08.016 · Cited by 274
Secondary structural ensembles of the SARS-CoV-2 RNA genome in infected cells
Lan, T. C. T., Allan, M. F., Malsick, L. E., Woo, J. Z., Zhu, C., Zhang, F., Khandwala, S., Nyeo, S. S. Y., Sun, Y., Guo, J. U., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28603-2 · Cited by 267
SARS-CoV-2 uses a multipronged strategy to impede host protein synthesis
Finkel, Y., Gluck, A., Nachshon, A., Winkler, R., Fisher, T., Rozman, B., Mizrahi, O., Lubelsky, Y., Zuckerman, B., Slobodin, B., et al. (2021) · Nature · doi:10.1038/s41586-021-03610-3 · Cited by 253
Innate immune evasion strategies of SARS-CoV-2
Minkoff, J. M., & tenOever, B. R. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00839-1 · Cited by 267
The molecular basis of translation initiation and its regulation in eukaryotes
Querido, J. B., Díaz‐López, I., & Ramakrishnan, V. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00624-9 · Cited by 269
Frere, J. J., Serafini, R. A., Pryce, K. D., Zazhytska, M., Oishi, K., Golynker, I., Panis, M., Zimering, J. H., Horiuchi, S., Hoagland, D. A., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abq3059 · Cited by 239
SARS‐CoV‐2 sensing by RIG‐I and MDA5 links epithelial infection to macrophage inflammation
Thorne, L., Reuschl, A., Zuliani‐Alvarez, L., Whelan, M. V. X., Turner, J. L. E., Noursadeghi, M., Jolly, C. L., & Towers, G. J. (2021) · The EMBO Journal · doi:10.15252/embj.2021107826 · Cited by 223
Rihn, S. J., Merits, A., Bakshi, S., Turnbull, M. L., Wickenhagen, A., Alexander, A. J. T., Baillie, C., Brennan, B., Brown, F., Brunker, K., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001091 · Cited by 212
Self-citationCheemarla, N. R., Watkins, T. A., Mihaylova, V. T., Wang, B., Zhao, D., Wang, G., Landry, M. L., & Foxman, E. F. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20210583 · Cited by 213
SARS-CoV-2 biology and host interactions
Steiner, S., Kratzel, A., Barut, G. T., Lang, R. M., Moreira, É. A., Thomann, L., Kelly, J. N., & Thiel, V. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-023-01003-z · Cited by 235
Zhou, Y., Liu, Y., Gupta, S., Paramo, M. I., Hou, Y., Mao, C., Luo, Y., Judd, J., Wierbowski, S. D., Bertolotti, M., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01474-0 · Cited by 214
Global Dynamics of Porcine Enteric Coronavirus PEDV Epidemiology, Evolution, and Transmission
Zhang, H., Zou, C., Peng, O., Ashraf, U., Xu, Q., Gong, L., Fan, B., Zhang, Y., Xu, Z., Xue, C., et al. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad052 · Cited by 208
Discovery and functional interrogation of SARS-CoV-2 RNA-host protein interactions
Flynn, R. A., Belk, J. A., Qi, Y., Yasumoto, Y., Wei, J., Alfajaro, M. M., Shi, Q., Mumbach, M. R., Limaye, A., DeWeirdt, P. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.012 · Cited by 206
Genome organization around nuclear speckles drives mRNA splicing efficiency
Bhat, P., Chow, A. Y., Emert, B. L., Ettlin, O., Quinodoz, S. A., Strehle, M. M., Takei, Y., Burr, A., Goronzy, I. N., Chen, A. W., et al. (2024) · Nature · doi:10.1038/s41586-024-07429-6 · Cited by 190
Self-citationThe SARS-CoV-2 RNA interactome
Lee, S., Lee, Y.-S., Choi, Y., Son, A., Park, Y., Lee, K., Kim, J., Kim, J., & Kim, V. N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.022 · Cited by 178
Tidu, A., Janvier, A., Schaeffer, L., Sosnowski, P., Kühn, L., Hammann, P., Westhof, É., Eriani, G., & Martin, F. (2020) · RNA · doi:10.1261/rna.078121.120 · Cited by 162
Kamel, W., Noerenberg, M., Cerikan, B., Chen, H., Järvelin, A. I., Kammoun, M., Lee, Y. S., Ni, S., García-Moreno, M., Andrejeva, A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.05.023 · Cited by 157
SARS-CoV-2 hijacks folate and one-carbon metabolism for viral replication
Zhang, Y., Guo, R., Kim, S. H., Shah, H., Zhang, S., Liang, J. H., Fāng, Y., Gentili, M., O'Leary, C. N., Elledge, S. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21903-z · Cited by 146
Yang, R., Deng, Y., Huang, B., Huang, L., Lin, A., Li, Y., Wang, W., Liu, J., Lu, S., Zhan, Z., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00634-z · Cited by 130
Self-citationSARS-CoV-2 viral proteins NSP1 and NSP13 inhibit interferon activation through distinct mechanisms
Vazquez, C., Swanson, S., Negatu, S. G., Dittmar, M., Miller, J., Ramage, H. R., Cherry, S. R., & Jurado, K. A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253089 · Cited by 124
Lin, J., Tang, C., Wei, H.-C., Du, B., Chen, C., Wang, M., Zhou, Y., Yu, M., Cheng, L., Kuivanen, S. H., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.015 · Cited by 116
Self-citationLim, J. M. E., Tan, A. T., Bert, N. L., Hang, S. K., Low, J. G. H., & Bertoletti, A. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20220780 · Cited by 115
Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets
Maio, N., Lafont, B. A. P., Sil, D., Li, Y., Bollinger, J. M., Jr., Krebs, C., Pierson, T. C., Linehan, W. M., & Rouault, T. A. (2021) · Science · doi:10.1126/science.abi5224 · Cited by 119
TOP1 inhibition therapy protects against SARS-CoV-2-induced lethal inflammation
Ho, J., Mok, B. W.-Y., Campisi, L., Jordan, T. X., Yildiz, S., Parameswaran, S., Wayman, J. A., Gaudreault, N. N., Meekins, D. A., Indran, S. V., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.051 · Cited by 121
Gioia, U., Tavella, S., Martínez-Orellana, P., Cicio, G., Colliva, A., Ceccon, M., Cabrini, M., Henriques, A. C., Fumagalli, V., Paldino, A., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01096-x · Cited by 120
Nuclear speckles – a driving force in gene expression
Faber, G. P., Nadav-Eliyahu, S., & Shav‐Tal, Y. (2022) · Journal of Cell Science · doi:10.1242/jcs.259594 · Cited by 114
Marchianò, S., Hsiang, T.-Y., Khanna, A., Higashi, T., Whitmore, L. S., Bargehr, J., Davaapil, H., Chang, J., Smith, E. A., Ong, L. P., et al. (2021) · Stem Cell Reports · doi:10.1016/j.stemcr.2021.02.008 · Cited by 112
Jachowicz, J. W., Strehle, M. M., Banerjee, A. K., Blanco, M. R., Thai, J., & Guttman, M. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00739-1 · Cited by 113
Self-citationLiu, X., Liang, W. P., Xu, F., Zhao, F., Huang, Y., Fan, Z., Mei, S., Hu, Y., Zhai, L., Guo, J., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abg8744 · Cited by 110
Kumar, A., Ishida, R., Strilets, T., Cole, J., López-Orozco, J., Fayad, N., Felix-Lopez, A., Elaish, M., Evseev, D., Magor, K. E., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00266-21 · Cited by 122
Mendez, A. S., Ly, M., González-Sánchez, A. M., Hartenian, E., Ingolia, N. T., Cate, J. H. D., & Glaunsinger, B. A. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109841 · Cited by 110
SARS-CoV-2 variants evolve convergent strategies to remodel the host response
Bouhaddou, M., Reuschl, A., Polacco, B. J., Thorne, L., Ummadi, M. R., Ye, C., Rosales, R., Pelin, A., Batra, J., Jang, G. Μ., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.026 · Cited by 120
Comprehensive mapping of SARS-CoV-2 interactions in vivo reveals functional virus-host interactions
Yang, S. L., DeFalco, L., Anderson, D. E., Zhang, Y., Aw, J. G. A., Lim, S. Y., Lim, X. N., Tan, K. Y., Zhang, T., Chawla, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25357-1 · Cited by 94
Mechanisms of Antiviral Immune Evasion of SARS-CoV-2
Beyer, D. K., & Forero, A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167265 · Cited by 96
Phase separation by the SARS-CoV-2 nucleocapsid protein: Consensus and open questions
Cascarina, S. M., & Ross, E. D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101677 · Cited by 91
Plasma miRNA profile at COVID-19 onset predicts severity status and mortality
Fernández-Pato, A., Virseda‐Berdices, A., Resino, S., Ryan, P., Martínez-Nieto, Ó., Pérez‐García, F., Martin‐Vicente, M., Valle‐Millares, D., Brochado‐Kith, O., Blancas, R., et al. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2038021 · Cited by 92
Guo, J. K., Blanco, M. R., Walkup, W. G., Bonesteele, G., Urbinati, C. R., Banerjee, A. K., Chow, A. Y., Ettlin, O., Strehle, M. M., Peyda, P., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.026 · Cited by 91
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Fisher, T., Gluck, A., Narayanan, K., Kuroda, M., Nachshon, A., Hsu, J. C., Halfmann, P., Yahalom-Ronen, Y., Tamir, H., Finkel, Y., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110954 · Cited by 87
Patrick, R., Janbandhu, V. C., Tallapragada, V. J., Tan, S. S. M., McKinna, E. E., Contreras, O., Ghazanfar, S., Humphreys, D. T., Murray, N. J., Tran, T. H. Y., et al. (2024) · Science Advances · doi:10.1126/sciadv.adk8501 · Cited by 96
Alfi, O., Yakirevitch, A., Wald, O., Wandel, O., Izhar, U., Oiknine‐Djian, E., Nevo, Y., Elgavish, S., Dagan, E., Madgar, O., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00130-21 · Cited by 81
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Ricardo-Lax, I., Luna, J. M., Thao, T. T. N., Pen, J. L., Yu, Y., Hoffmann, H.-H., Schneider, W. M., Razooky, B. S., Fernández-Martínez, J., Schmidt, F., et al. (2021) · Science · doi:10.1126/science.abj8430 · Cited by 80
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Pawlica, P., Yario, T. A., White, S., Wang, J., Moss, W. N., Hui, P., Vinetz, J. M., & STEITZ, J. A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116668118 · Cited by 84
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Nakagawa, K., & Makino, S. (2021) · Cells · doi:10.3390/cells10020300 · Cited by 78
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Bastard, P., Zhang, Q., Zhang, S., Jouanguy, E., & Casanova, J. (2022) · Current Opinion in Immunology · doi:10.1016/j.coi.2022.01.003 · Cited by 73
Zhou, H., Møhlenberg, M., Thakor, J. C., Tuli, H. S., Wang, P., Assaraf, Y. G., Dhama, K., & Jiang, S. (2022) · Clinical Microbiology Reviews · doi:10.1128/cmr.00014-22 · Cited by 78
Veleri, S. (2021) · Experimental Brain Research · doi:10.1007/s00221-021-06244-z · Cited by 77
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Farley, S. E., Kyle, J. E., Leier, H. C., Bramer, L., Weinstein, J. B., Bates, T. A., Lee, J., Metz, T., Schultz, C., & Tafesse, F. (2022) · Nature Communications · doi:10.1038/s41467-022-31097-7 · Cited by 75
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Yuan, S., Balaji, S., Lomakin, I. B., & Xiong, Y. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.752214 · Cited by 69
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Labeau, A., Fery-Simonian, L., Lefèvre‐Utile, A., Pourcelot, M., Bonnet‐Madin, L., Soumelis, V., Lotteau, V., Vidalain, P., Amara, A., & Meertens, L. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110744 · Cited by 75
Mapping and engineering RNA-driven architecture of the multiphase nucleolus
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Self-citationViral-induced alternative splicing of host genes promotes influenza replication
Thompson, M. G., Dittmar, M., Mallory, M. J., Bhat, P., Ferretti, M., Fontoura, B. M. A., Cherry, S. R., & Lynch, K. W. (2020) · eLife · doi:10.7554/elife.55500 · Cited by 66
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Bocci, M., Oudenaarden, C., Saenz-Sardà, X., Simrén, J., Edén, A., Sjölund, J., Möller, C., Gisslén, M., Zetterberg, H., Englund, E. M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111622 · Cited by 68
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Grellet, E., L’Hote, I., Goulet, A., & Imbert, I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101923 · Cited by 71
SARS-CoV-2 infection of sustentacular cells disrupts olfactory signaling pathways
Verma, A. K., Zheng, J. H., Meyerholz, D. K., & Perlman, S. M. (2022) · JCI Insight · doi:10.1172/jci.insight.160277 · Cited by 76
siRNA Therapeutics for the Therapy of COVID-19 and Other Coronaviruses
Sajid, M. I., Moazzam, M., Cho, Y., Kato, S., Xu, A., Way, J. J., Lohan, S., & Tiwari, R. K. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c01239 · Cited by 64
Rao, S. J., Hoskins, I., Tonn, T., Garcia, P. D., Özadam, H., Cenik, E. S., & Cenik, C. (2021) · RNA · doi:10.1261/rna.078661.120 · Cited by 63
SARS-CoV-2 Subgenomic RNAs: Characterization, Utility, and Perspectives
Long, S. (2021) · Viruses · doi:10.3390/v13101923 · Cited by 67
The key features of SARS-CoV-2 leader and NSP1 required for viral escape of NSP1-mediated repression
Bujanic, L., Shevchuk, O., von Kügelgen, N., Kalinina, A., Ludwik, K. A., Koppstein, D., Zerna, N., Sickmann, A., & Chekulaeva, M. (2022) · RNA · doi:10.1261/rna.079086.121 · Cited by 62
Immune evasion of SARS-CoV-2 from interferon antiviral system
Min, Y., Huang, M., Sun, X., Dèng, F., Wáng, H., & Ning, Y. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.023 · Cited by 65
SARS-CoV-2 Non-Structural Proteins and Their Roles in Host Immune Evasion
Low, Z. Y., Zabidi, N. Z., Yip, A. J. W., Puniyamurti, A., Chow, V. T. K., & Lal, S. K. (2022) · Viruses · doi:10.3390/v14091991 · Cited by 68
Translational control of coronaviruses
de Breyne, S., Vindry, C., Guillin, O., Condé, L., Mure, F., Gruffat, H., Chavatte, L., & Ohlmann, T. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1116 · Cited by 61
The molecular mechanism of SARS-CoV-2 evading host antiviral innate immunity
Gu, W., Gan, H., Ma, Y., Xu, L., Cheng, Z. J., Li, B., Zhang, X., Jiang, W., Sun, J., Sun, B., et al. (2022) · Virology Journal · doi:10.1186/s12985-022-01783-5 · Cited by 64
Transient and stabilized complexes of Nsp7, Nsp8, and Nsp12 in SARS-CoV-2 replication
Wilamowski, M., Hammel, M., Leite, W. C., Zhang, Q., Kim, Y., Weiss, K. L., Jedrzejczak, R. P., Rosenberg, D. J., Fan, Y., Wower, J., et al. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.06.006 · Cited by 60
Interferon induction, evasion, and paradoxical roles during SARS‐CoV‐2 infection*
Chiale, C., Greene, T. T., & Zúñiga, E. I. (2022) · Immunological Reviews · doi:10.1111/imr.13113 · Cited by 66
Delivery Routes for COVID-19 Vaccines
Park, J. H., & Lee, H. K. (2021) · Vaccines · doi:10.3390/vaccines9050524 · Cited by 53
SARS-CoV-2 Nsp14 mediates the effects of viral infection on the host cell transcriptome
Zaffagni, M., Harris, J. M., Patop, I. L., Pamudurti, N. R., Nguyen, S., & Kadener, S. (2022) · eLife · doi:10.7554/elife.71945 · Cited by 58
Characterization of SARS-CoV-2 Evasion: Interferon Pathway and Therapeutic Options
Znaidia, M., Demeret, C., van der Werf, S., & Komarova, A. V. (2022) · Viruses · doi:10.3390/v14061247 · Cited by 57
Jungreis, I., Nelson, C. W., Ardern, Z., Finkel, Y., Krogan, N. J., Sato, K., Ziebuhr, J., Stern‐Ginossar, N., Pavesi, A., Firth, A. E., et al. (2021) · Virology · doi:10.1016/j.virol.2021.02.013 · Cited by 57
Structural Plasticity and Immune Evasion of SARS-CoV-2 Spike Variants
Ghimire, D., Han, Y., & Lu, M. (2022) · Viruses · doi:10.3390/v14061255 · Cited by 44
Littler, D. R., Liu, M., McAuley, J., Lowery, S. A., Illing, P. T., Gully, B. S., Purcell, A. W., Chandrashekaran, I. R., Perlman, S. M., Purcell, D. F. J., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101362 · Cited by 51
Slobodin, B., Sehrawat, U., Lev, A. I., Hayat, D., Zuckerman, B., Fraticelli, D., Ogran, A., Ben‐Shmuel, A., Bar-David, E., Levy, H., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac615 · Cited by 49
A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures
Liang, X., Xiao, J. H., Li, X., Liu, Y., Lu, Y. P., Wen, Y., Li, Z., Che, X., Ma, Y., Zhang, X., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01128-x · Cited by 47
SND1 binds SARS-CoV-2 negative-sense RNA and promotes viral RNA synthesis through NSP9
Schmidt, N., Ganskih, S., Wei, Y., Gabel, A., Zielinski, S., Keshishian, H., Lareau, C. A., Zimmermann, L., Makroczyová, J., Pearce, C., et al. (2023) · Cell · doi:10.1016/j.cell.2023.09.002 · Cited by 48
Interfering with SARS-CoV-2: are interferons friends or foes in COVID-19?
Zanoni, I. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.004 · Cited by 49
An, S., Li, Y., Lin, Y., Chu, J., Su, J., Chen, Q., Wang, H., Pan, P., Zheng, R., Li, J., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.756288 · Cited by 46
Viral evasion of the interferon response at a glance
Zhu, J., Chiang, C., & Gack, M. U. (2023) · Journal of Cell Science · doi:10.1242/jcs.260682 · Cited by 50
Decoding protein–RNA interactions using CLIP-based methodologies
Xiang, J. S., Schafer, D. M., Rothamel, K. L., & Yeo, G. W.-M. (2024) · Nature Reviews Genetics · doi:10.1038/s41576-024-00749-3 · Cited by 50
Impact of remdesivir according to the pre-admission symptom duration in patients with COVID-19
García‐Vidal, C., Alonso, R., Camon, A. M., Cardozo, C., Albiach, L., Agüero, D. L., Marcos, M. Á., Ambrosioni, J., Bodro, M., Chumbita, M., et al. (2021) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkab321 · Cited by 47
Li, W., Yang, S., Xu, P., Zhang, D., Tong, Y., Chen, L., Jia, B., Li, A., Lian, C., Ru, D., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103861 · Cited by 46
Self-citationMechanisms contributing to adverse outcomes of COVID-19 in obesity
Sudhakar, M., Beaula, W. S., Meiyazhagan, G., & Parvathi, V. D. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04356-w · Cited by 50
I(nsp1)ecting SARS-CoV-2–ribosome interactions
Simeoni, M., Cavinato, T., Rodríguez, D., & Gatfield, D. (2021) · Communications Biology · doi:10.1038/s42003-021-02265-0 · Cited by 45
Li, T., Wen, Y., Guo, H., Yang, T., Yang, H., & Ji, X. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.813248 · Cited by 45
Causes and Consequences of Purifying Selection on SARS-CoV-2
Castillo-Morales, A., Rice, A. M., Ho, A. T., Mordstein, C., Mühlhausen, S., Watson, S., Cano, L., Young, B., Kudla, G., & Hurst, L. D. (2021) · Genome Biology and Evolution · doi:10.1093/gbe/evab196 · Cited by 43
Prokop, J. W., Hartog, N., Chesla, D. W., Faber, W., Love, C. P., Karam, R., Abualkheir, N., Feldmann, B., Teng, L., McBride, T., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.694243 · Cited by 40
ACE2-lentiviral transduction enables mouse SARS-CoV-2 infection and mapping of receptor interactions
Rawle, D. J., Le, T. T., Dumenil, T. D., Yan, K., Tang, B., Nguyen, W., Watterson, D., Modhiran, N., Hobson‐Peters, J., Bishop, C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009723 · Cited by 41
Metadata
- 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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