Cited by 957interferon and immune responsesSARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections Studies

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Evasion of Type I Interferon by SARS-CoV-2

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Xia, Hongjie, Cao, Zengguo, Xie, Xuping, Zhang, Xianwen, Chen, John Yun-Chung, Wang, Hualei, Menachery, Vineet D., Rajsbaum, Ricardo, Shi, Pei-Yong·2020·Cell Reports

DOI 10.1016/j.celrep.2020.108234PMC PMC7501843

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Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) replication and host immune response determine coronavirus disease 2019 (COVID-19), but studies evaluating viral evasion of immune response are lacking. Here, we use unbiased screening to identify SARS-CoV-2 proteins that antagonize type I interferon (IFN-I) response. We found three proteins that antagonize IFN-I production via distinct mechanisms: nonstructural protein 6 (nsp6) binds TANK binding kinase 1 (TBK1) to suppress interferon regulatory factor 3 (IRF3) phosphorylation, nsp13 binds and blocks TBK1 phosphorylation, and open reading frame 6 (ORF6) binds importin Karyopherin α 2 (KPNA2) to inhibit IRF3 nuclear translocation. We identify two sets of viral proteins that antagonize IFN-I signaling through blocking signal transducer and activator of transcription 1 (STAT1)/STAT2 phosphorylation or nuclear translocation. Remarkably, SARS-CoV-2 nsp1 and nsp6 suppress IFN-I signaling more efficiently than SARS-CoV and Middle East respiratory syndrome coronavirus (MERS-CoV). Thus, when treated with IFN-I, a SARS-CoV-2 replicon replicates to a higher level than chimeric replicons containing nsp1 or nsp6 from SARS-CoV or MERS-CoV. Altogether, the study provides insights on SARS-CoV-2 evasion of IFN-I response and its potential impact on viral transmission and pathogenesis.

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Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro
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Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., et al. (2006) · Nature · doi:10.1038/nature04734 · Cited by 3,888
STATs: transcriptional control and biological impact
Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201
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Mahajan, S., Choudhary, S., Kumar, P., & Tomar, S. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116356 · Cited by 127
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Lim, 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
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Uversky, V. N., Redwan, E. M. M. M., Makis, W., & Rubio‐Casillas, A. (2023) · Vaccines · doi:10.3390/vaccines11050991 · Cited by 127
Sensing of cytoplasmic chromatin by cGAS activates innate immune response in SARS-CoV-2 infection
Zhou, Z. L., Zhang, X., Lei, X., Xiao, X., Jiao, T., Ma, R., Dong, X., Jiang, Q., Wang, W., Shi, Y., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00800-3 · Cited by 120
Self-citation
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Arshad, N., Laurent-Rolle, M., Ahmed, W. S., Hsu, J. C.-C., Mitchell, S. M., Pawlak, J., Sengupta, D., Biswas, K. H., & Cresswell, P. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208525120 · Cited by 119
A dual-role of SARS-CoV-2 nucleocapsid protein in regulating innate immune response
Zhao, Y., Sui, L., Wu, P., Wang, W., Wang, Z., Yu, Y., Hou, Z., Tan, G., Liu, Q., & Wang, G. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00742-w · Cited by 114
SARS-CoV-2 spike protein–induced cell fusion activates the cGAS-STING pathway and the interferon response
Liu, 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
Physiological functions of RIG-I-like receptors
Yoneyama, M., Kato, H., & Fujita, T. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.003 · Cited by 117
SARS-CoV-2 Nonstructural Protein 1 Inhibits the Interferon Response by Causing Depletion of Key Host Signaling Factors
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
Regulation of antiviral innate immune signaling and viral evasion following viral genome sensing
Chathuranga, K., Weerawardhana, A., Dodantenna, N., & Lee, J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00691-y · Cited by 110
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Thorne, L. G., Bouhaddou, M., Reuschl, A.-K., Zuliani-Alvarez, L., Polacco, B., Pelin, A., Batra, J., Whelan, M. V. X., Ummadi, M., Rojc, A., et al. (2021) · doi:10.1101/2021.06.06.446826 · Cited by 91
SARS‐CoV‐2 ORF10 antagonizes STING‐dependent interferon activation and autophagy
Han, L., Zheng, Y., Deng, J., Nan, M., Xiao, Y., Zhuang, M., Zhang, J., Wang, W. J., Gao, C., & Wang, P. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27965 · Cited by 109
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Sun, S., Gu, H., Cao, L., Chen, Q., Ye, Q., Yang, G., Li, R.-T., Fan, H., Deng, Y.-Q., Song, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25903-x · Cited by 104
Self-citation
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Kakavandi, S., Zare, I., Vaezjalali, M., Dadashi, M., Azarian, M., Akbari, A., Farani, M. R., Zalpoor, H., & Hajikhani, B. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01104-5 · Cited by 110
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Zaid, Y., Doré, É., Dubuc, I., Archambault, A., Flamand, O., Laviolette, M., Flamand, N., Boilard, É., & Flamand, L. (2021) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2021.05.032 · Cited by 100
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Liu, Y., Zhang, X., Liu, J., Xia, H., Zou, J., Muruato, A. E., Periasamy, S., Kurhade, C., Plante, J. A., Bopp, N. E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31930-z · Cited by 92
Self-citation
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Zandi, M., Shafaati, M., Kalantar-Neyestanaki, D., Pourghadamyari, H., Fani, M., Soltani, S., Kaleji, H., & Abbasi, S. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113889 · Cited by 85
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Seifert, M., Bera, S. C., van Nies, P., Kirchdoerfer, R. N., Shannon, A., Le, T.-T.-N., Meng, X., Xia, H., Wood, J. M., Harris, L. D., et al. (2021) · eLife · doi:10.7554/elife.70968 · Cited by 91
Self-citation
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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
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Grifoni, A., Alonzi, T., Alter, G., Noonan, D. M., LANDAY, A. L., Albini, A., & Goletti, D. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1146704 · Cited by 90
The roles of signaling pathways in SARS-CoV-2 infection; lessons learned from SARS-CoV and MERS-CoV
Hemmat, N., Asadzadeh, Z., Ahangar, N. K., Alemohammad, H., Najafzadeh, B., Derakhshani, A., Baghbanzadeh, A., Baghi, H. B., Javadrashid, D., Najafi, S., et al. (2021) · Archives of Virology · doi:10.1007/s00705-021-04958-7 · Cited by 81
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Chen, D. W., Khan, N., Close, B. J., Goel, R. K., Blum, B. C., Tavares, A. H., Kenney, D., Conway, H. L., Ewoldt, J. K., Chitalia, V. C., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00862-21 · Cited by 81
Impact of SARS-CoV-2 ORF6 and its variant polymorphisms on host responses and viral pathogenesis
Kehrer, T., Čupić, A., Ye, C., Yildiz, S., Bouhaddou, M., Crossland, N. A., Barrall, E. A., Cohen, P., Tseng, A. E., Çağatay, T., et al. (2023) · Cell Host & Microbe · doi:10.1016/j.chom.2023.08.003 · Cited by 87

Authors: Xia, H., Cao, Z., Xie, X., Zhang, X., Chen, J. Y.-C., Wang, H., Menachery, V. D., Rajsbaum, R., & Shi, P.-Y.
Affiliations: The University of Texas Medical Branch at Galveston (US)
Jilin University (CN)
Corresponding author: Xia, Hongjie
Shi, Pei-Yong
ORCID: Xia, Hongjie
Xie, Xuping
Zhang, Xianwen
Wang, Hualei
Menachery, Vineet D.
Rajsbaum, Ricardo
Shi, Pei-Yong
Venue: Cell Reports
Publisher: Elsevier BV
Published: 2020-10
Volume: 33
Issue: 1
Pages: 108234
ISSN: 2211-1247 (ISSN-L)
DOI: 10.1016/j.celrep.2020.108234
PMC: PMC7501843
OpenAlex: W3087744389
Cited by: 957
References: 55
Citations by year: 2026: 36 · 2025: 79 · 2024: 116 · 2023: 167 · 2022: 253 · 2021: 266 · 2020: 40
FWCI: 63.58
Type: journal article
Language: en
Open access: gold
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 Reports (publishedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: National Institutes of Health (AI142759, AI134907, AI145617, UL1TR001439)
Summerfield G. Roberts Foundation (R01AI134907, R21AI126012-01A1, R21AI132479-01, R00AG049092, U19AI100625, R24AI120942)
Sealy and Smith Foundation
John S. Dunn Foundation
Gillson Longenbaugh Foundation
Amon G. Carter Foundation
University of Texas System
Robert J. Kleberg, Jr. and Helen C. Kleberg Foundation
Topics: Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Keywords: SARS-CoV-2, interferon signaling, NSP6, nsp13, ORF6, TBK1, IRF3 phosphorylation, KPNA2, Nsp1, viral immune evasion, COVID-19 pandemic, SARS-CoV, MERS-CoV, viral replication
MeSH terms: A549 Cells, Betacoronavirus, COVID-19, SARS-CoV-2, Coronavirus Nucleocapsid Proteins, Animals, Cricetulus, Cricetinae, Humans, Interferon Type I, Methyltransferases, Pneumonia, Viral, Protein Binding, Viral Proteins, Protein Serine-Threonine Kinases, Viral Nonstructural Proteins, Coronavirus Infections, RNA Helicases, alpha Karyopherins, Capsid Proteins, STAT Transcription Factors, Interferon Regulatory Factor-3, Immune Evasion, HEK293 Cells, Pandemics

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