The DOI matches its Crossref record; 52 of the 55 references it cites were found in a registry or an index, and 2 are not checked yet.
Evasion of Type I Interferon by SARS-CoV-2
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Functional testing further supported the counteracting activity of ORF3b, ORF6, NSP1, or NSP13 on type I IFN activation, of which particularly ORF6 suppressed STAT1 and STAT2 phosphorylation and STAT1 nuclear translocation, (Konno et al., 2020; Lei et al., 2020; Xia et al., 2020).”
From COVID-19 and the human innate immune system (2021) · cites this paper as Xia et al., 2020
In the citing paper
“Interaction mapping further suggested that NSP13 interacts with TBK1, NSP15 with NRDP1 (an E3 ubiquitin ligase controlling the balance between JAK2-associated cytokine receptor degradation and ectodomain shedding), ORF9b with TOMM70 (an important receptor of the outer mitochondrial membrane), and ORF6 with either KPNA2 or the IFN-induced NUP98-RAE1 nuclear export complex, which are both involved”
From COVID-19 and the human innate immune system (2021) · cites this paper as Xia et al., 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China
Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884
Self-citationA novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
Self-citationWu, Z., & McGoogan, J. M. (2020) · JAMA · doi:10.1001/jama.2020.2648 · Cited by 17,016
Wang, M., Cao, R., Zhang, L., Yang, X., Liu, J., Xu, M., Shi, Z., Hú, Z., Zhong, W., & Xiao, G. (2020) · Cell Research · doi:10.1038/s41422-020-0282-0 · Cited by 6,994
Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
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
Interferon-stimulated genes: A complex web of host defenses
Schneider, W. M., Chevillotte, M. D., & Rice, C. M. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120231 · Cited by 3,067
Antiviral Actions of Interferons
Samuel, C. E. (2001) · Clinical Microbiology Reviews · doi:10.1128/cmr.14.4.778-809.2001 · Cited by 2,743
IKKε and TBK1 are essential components of the IRF3 signaling pathway
Fitzgerald, K. A., McWhirter, S. M., Faia, K. L., Rowe, D. C., Latz, E., Golenbock, D. T., Coyle, A. J., Liao, S.-M., & Maniatis, T. (2003) · Nature Immunology · doi:10.1038/ni921 · Cited by 2,680
Flagged first, then by citations
1 of the 55 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Lokugamage, 2020, SARS-CoV-2 is sensitive to type I interferon pretreatment, bioRxiv
Cited by
Sorted by citations
Items 901–956 of 956
Byun, W. G., Lee, M., Ko, M., Lee, J. H., Yi, S., Lee, J., Kim, S., & Park, S. B. (2024) · Angewandte Chemie · doi:10.1002/ange.202405472
Iyer, V. A., Mohan, A., Kumar, D., & Dahiya, P. (2024) · COVID · doi:10.3390/covid4090100
Novel Design for Multi-Epitope Vaccines of COVID-19 and Critical In silico Assessment Steps
Lan, T., Su, S., Ping, P., & Li, J. (2024) · Current Bioinformatics · doi:10.2174/0115748936303461240827061629
Human cellular restriction factors that target SARS-CoV-2 replication
Marivate, A., Bekker, S., Fish, M. Q., & Mosebi, S. (2024) · Frontiers in Virology · doi:10.3389/fviro.2024.1462283
Vu, L. D., Christofferson, R. C., O’Neal, H. R., Hamer, D., Phan, A., Vance, K. M., Turner, E. A., Kumar, A., Yola, I. M., Lim, N., et al. (2024) · Experimental Biology and Medicine · doi:10.3389/ebm.2024.10193
Elegant and Innovative Recoding Strategies for Advancing Vaccine Development
Meurens, F., Renois, F., & Karniychuk, U. U. (2025) · Vaccines · doi:10.3390/vaccines13010078
Types of effects of SARS-CoV-2 on the human body: from coagulopathy to cytokine storm
Михайлович, Н. К., Yakovleva, S. A., Shrayner, E. V., Platonova, P. Y., Novikova, M., Tumas, A. S., Евгеньевна, В. Е., Lukichev, D. A., Sergeev, D., Хавкин, А. И., et al. (2025) · Vrach · doi:10.29296/25877305-2025-03-02
Pearl, R., Francina, M. D., Raymond, M. T., Guler, R., Matsebatlela, T. M., & Makena, W. M. H. (2025) · Research Square · doi:10.21203/rs.3.rs-6228859/v1
Cytoplasmic Viral RNA Sensors: RIG-I-Like Receptors
Kato, H., Tsukamoto, Y., & Fujita, T. (2025) · Elsevier eBooks · doi:10.1016/b978-0-12-824465-4.00182-4
Sima, S. T., Puebla-Clark, L., González-Orozco, M., Endrino, M. J., Shelite, T. R., Hsiang-Chi, T., Martinez-Martinez, Y. B., Huante, M. B., Federman, H. G., Gbédandé, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.13.653138
Self-citationDifferential response of human plasmacytoid pre-dendritic cells to SARS-CoV-2 variants
Kartasheva-Ebertz, D., Topalis, D., Umaña-Diaz, C., Ayas, O., Couture, L., Tonnerre, P., Medvedovic, J., Meertens, L., Soumelis, V., & Amara, A. (2025) · iScience · doi:10.1016/j.isci.2025.113394
Cabrera-Serrano, A. J., Ruiz-Durán, L., Gutiérrez‐Bautista, J. F., Carretero-Fernández, M., ter Horst, R., Li, Y., Reyes‐Zurita, F. J., García‐Verdejo, F. J., Netea, M. G., Sánchez‐Rovira, P., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1639825
Gracias, S., Seac’h, E. L., Donaire-Carpio, S., Vuillier, F., Vendramini, L., Moundib, A., Temmam, S., Rutkowska, M., Donati, F., Čupić, A., et al. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013573
Suffredini, A. F., Gairhe, S., Xu, L., Kanth, S. M., Huapaya, J. A., Demirkale, C. Y., Regenold, D., Turan, S., Chimukangara, B., Strich, J. R., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-7716872/v1
Pathogenetic Predictors of Complications of the New Coronavirus Infection SARS-COV-2
Chepur, S. V., Nn, P., Chubar, O. V., Сергеевна, Б. Л., Litvinenko, I., Tjunin, M. A., Mjasnikova, I. A., & Пугач, В. А. (2025) · Biology Bulletin Reviews · doi:10.1134/s2079086425600110
Zhong, C., She, G., Zhao, Y., Liu, Y., Liu, J., Wei, X., Chen, Z., Zhao, K., Zhao, Z., Zhichao, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25566274
Acosta, G. A. A., Chávez, M. A. C. M., Martínez-Quezada, R. M.-Q., Rodríguez, C. E. M., Reyes-Montes, M. D. R., Sánchez-Conejo, A. R., & Valencia-Ledezma, O. E. (2023) · Research Square · doi:10.21203/rs.3.rs-3161655/v1
Zhong, C., She, G., Zhao, Y., Liu, Y., Liu, J., Wei, X., Chen, Z., Zhao, K., Zhao, Z., Zhichao, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25566379
Molecular signature of COVID-19 prior to its exacerbation by multi-omics surveyPreprint
Suzuki, T., Kita, Y., Yanagida, K., Maeda, K., Hashidate‐Yoshida, T., Nakanishi, H., Ohto‐Nakanishi, T., Terada-Hirashima, J., Tsujimoto, Y., Hojo, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.27.696524
Antonika, C., Ojha, D., & Danthi, P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.08.698360
Development of a stable replicon system of a pangolin merbecovirus for antiviral screening
Wu, C., Wang, J.-H., Zhu, B., & Chen, J. (2026) · Virologica Sinica · doi:10.1016/j.virs.2026.02.004
Self-citationZhang, Y., & Stevenson, N. J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1739662
Liu, X., Ssemadaali, M. A., Radhakrishnan, H., Arredondo, J., Javitz, H. S., Dandekar, S., & Bhatnagar, P. (2026) · Molecular Medicine · doi:10.1186/s10020-025-01420-1
Caractérisation des activités antivirales des anticorps anti-VIH-1 et anti-SARS-CoV-2
Dufloo, J. (2021) · theses.fr (ABES) · doi:10.70675/215798eaz7f82z4e57za8eazf4453d37b8c8
From inborn errors of type I interferon immunity to their auto-immune phenocopy
Bastard, P. (2021) · theses.fr (ABES) · doi:10.70675/f5317e13z2706z4560zbdaaz9a46de0b5fc7
Martin, M. F. (2021) · theses.fr (ABES) · doi:10.70675/e60e954czb686z4463z8169z3023a8d8e4c3
Morin‐Dewaele, M. (2023) · theses.fr (ABES) · doi:10.70675/3332ee05z67cez489cza3e8zb3843eed7d42
The role of O-GlcNAcylation in the pathophysiology of Systemic Lupus Erythematosus
Galli, G. (2022) · theses.fr (ABES) · doi:10.70675/db863337z7c69z4a5dz9e94z7163b54542ee
Single cell monitoring of antiviral response regulation upon viral infection
Ribeiro, M. M. S. (2022) · theses.fr (ABES) · doi:10.70675/ad14ca1bzc138z439ezaea2z978adb91e70c
Mécanismes des pertes de l'odorat associées à la COVID-19 sur le modèle hamster doré syrien
Bourgon, C. (2023) · theses.fr (ABES) · doi:10.70675/69199ab8z58f9z41c1za0cbz3ce0351309f8
Pesenti, L. (2024) · theses.fr (ABES) · doi:10.70675/04a80eeazdd63z42e4zbd7fz230cf5dbc199
Étude de la réponse humorale lors de l'infection par le SARS-CoV-2
Marot, S. (2023) · theses.fr (ABES) · doi:10.70675/7d41e61azd818z408dzb17cz1c0cf0738b83
Citrus-derived peptides: Emerging functional and therapeutic potential
Akbari, B., & Gashti, M. P. (2026) · Food Bioscience · doi:10.1016/j.fbio.2026.108841
Xu, J., Xiao, Y., Lu, W., Song, Z., Zhou, L., Gao, Q., Xu, X., Shan, Y., Fang, W., Zhao, L., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152211
Ugbaja, S. C., Nkabinde, S. A., Nkabinde, M., & Gqaleni, N. (2026) · Biomedicines · doi:10.3390/biomedicines14051022
Maddaloni, L., Tirelli, V., Bugani, G., Santinelli, L., Fracella, M., Picozza, M., Cavallari, E. N., Ceccarelli, G., Antonelli, G., Mastroianni, C. M., et al. (2026) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.71190
Kim, Y. W., Lee, S. J., Lee, W. M., Kim, S.-J., & Ahn, D. (2026) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2602.02038 · Cited by 1
Suphatrakul, A., Chantima, W., Posiri, P., Srisuk, N., Nantachokechawapan, R., Panyain, N., Onnome, S., Rotchanapreeda, T., Thanatummatis, B., Sittisombut, N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.04.729841
Fu, J., Mi, Z., & Li, Z. Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1796416
NAE inhibitor MLN4924 effectively suppresses Coxsackievirus B3 replication
Li, S. W., Wei, J., Dong, Y., Luan, T., Feng, D., Wang, X., Wang, Z., Zhao, Y., Yang, B., Wang, Y., et al. (2026) · Microbial Pathogenesis · doi:10.1016/j.micpath.2026.108648
A fungal-induced immune response that mediates resistance against COVID-19
de Souza, R. L. L., Benevides, L., Rigoni, T. S., Abuna, R. P. F., Rattis, B. A. D. C., Nonato, O. C. D. S., Bocca, A. L., Gazzinelli, R. T., & Silva, J. S. (2026) · Journal of Microbiology Immunology and Infection · doi:10.1016/j.jmii.2026.06.007
Yu, Y., He, W., Geng, X., He, Y., Feng, H., Chen, J., & Shu, J. (2026) · Viruses · doi:10.3390/v18070721
Self-citationSARS-CoV-2 NSP8-Derived Peptide Effectively Suppresses the Activity of Helicase NSP13
Pashova, S., Petkov, P., Hristova, R., Krachmarova, E., Nacheva, G. A., Gospodinov, A. G., Lilkova, E., Ilieva, N., Rangelov, M. A., Todorova, N. H., et al. (2026) · Computational and Structural Biotechnology Journal · doi:10.34133/csbj.0174
Angamarca-Iguago, J., Parise-Vasco, J. M., Reytor-González, C., Cagua-Ordoñez, J. C., & Simancas‐Racines, D. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27135994
Conformational bias in SARS-CoV-2 Spike CD4+ T-cell epitope dominance
Landry, S. J., Steede, N. K., Tiomkin, Y., Smith, H., Mettu, R. R., Gragert, L. A., Aberle, J. H., Zwezdaryk, K. J., Zheng, C., Kolls, J. K., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1857103
Molecular signature of COVID-19 prior to its exacerbation by multi-omics survey
Suzuki, T., Kita, Y., Yanagida, K., Maeda, K., Hashidate‐Yoshida, T., Nakanishi, H., Ohto‐Nakanishi, T., Terada-Hirashima, J., Tsujimoto, Y., Hojo, M., et al. (2026) · PLoS ONE · doi:10.1371/journal.pone.0352423
Khan, N., Lani, R., & Hassandarvish, P. (2026) · Future Virology · doi:10.1080/17460794.2026.2713361
Immune Responses to Severe Acute Respiratory Syndrome Coronavirus-2
Kaushal, H., & Mittal, P. (2026) · Springer eBooks · doi:10.1007/978-3-032-26000-0_9
Zhang, G., Lai, Y., & Zhao, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1934930
Interferon crosstalk at the lung barrier in viral and fungal infection
Brochero, M. I. V., & Rivera, A. (2026) · Infection and Immunity · doi:10.1128/iai.00295-26
Lin, D., Yeh, F.-C., Su, Y.-S., Hsu, Y.-S., Chang, M., & Huang, S.-W. (2026) · Journal of microbiology, immunology, and infection = Wei mian yu gan ran za zhi · doi:10.1016/j.jmii.2026.09.010
Hitting Coronaviruses Where It Hurts: Antiviral Strategies Targeting Viral Proteins
de la Cruz‐Potenciano, A., Maldonado, M., Camarasa, M., & de Castro, S. (2026) · ChemMedChem · doi:10.1002/cmdc.70507
Fu, J., & Li, Z. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1995184
SARS‐CoV‐2 ORF6 protein targets IFP35 to inhibit the IFNγ signaling pathway
Liu, L., Du, J., Huang, J., Yang, S., Xiao, Q., Cao, L., Peng, H., Zheng, B., Li, C., & 郭德银 (2026) · mLife · doi:10.1002/mlf2.70112
Metadata
- 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
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2020-10
- Volume
- 33
- Issue
- 1
- Pages
- 108234
- ISSN
- 2211-1247 (ISSN-L)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
