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Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses
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Abstract
Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.
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“SARS-CoV-2 is a single-stranded RNA β-coronavirus and a member of the subgenus Sarbecovirus (beta-CoV lineage B).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“The S protein mediates binding of coronaviruses to angiotensin converting enzyme 2 (ACE2) on the surface of various cell types including epithelial cells of the pulmonary alveolus (4–6).”
From An Alphavirus -derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates (2020) · cites this paper as [5]
Experimental — accuracy not yet measuredIn the citing paper
“it directly interacts with the cellular receptor angiotensin converting enzyme 2 (ACE2) which mediates host cell entry”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Letko et al., 2020
In the citing paper
“It is the seventh member of the Coronaviridae known to infect humans so far, two of which, SARS-CoV and MERS-CoV, caused global health threats previously (Guarner, 2020; Letko et al., 2020).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
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Cites
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
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F. (2020) · Journal of Virology · doi:10.1128/jvi.00127-20 · Cited by 4,341
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740
Bats Are Natural Reservoirs of SARS-Like Coronaviruses
Li, W., Shi, Z., Yu, M., Ren, W., Smith, C. S., Epstein, J. H., Wang, H., Crameri, G. S., Hú, Z., Zhang, H., et al. (2005) · Science · doi:10.1126/science.1118391 · Cited by 2,571
Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
Raj, V. S., Mou, H., Smits, S. L., Dekkers, D. H. W., Müller, M. A., Dijkman, R., Muth, D., Demmers, J. A. A., Zaki, A., Fouchier, R. A. M., et al. (2013) · Nature · doi:10.1038/nature12005 · Cited by 2,061
Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Li, F., Li, W., Farzan, M., & Harrison, S. C. (2005) · Science · doi:10.1126/science.1116480 · Cited by 2,035
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778
Severe acute respiratory syndrome coronavirus-like virus in Chinese horseshoe bats
Lau, S. K. P., Woo, P. C. Y., Li, K. S. M., Huang, Y. P., Tsoi, H., Wong, B. H. L., Wong, S. S. Y., Leung, S.-Y., Chan, K., & Yuen, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506735102 · Cited by 1,561
Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,076
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Car, Z., Šegota, S. B., Anđelić, N., Lorencin, I., & Mrzljak, V. (2020) · Computational and Mathematical Methods in Medicine · doi:10.1155/2020/5714714 · Cited by 206
Fignani, D., Licata, G., Brusco, N., Nigi, L., Grieco, G. E., Marselli, L., Overbergh, L., Gysemans, C. A., Colli, M. L., Marchetti, P., et al. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.596898 · Cited by 219
Establishment of an African green monkey model for COVID-19 and protection against re-infection
Woolsey, C. B., Borisevich, V., Prasad, A. N., Agans, K. N., Deer, D. J., Dobias, N. S., Heymann, J. C., Foster, S. L., Levine, C. B., Medina, L. O., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-00835-8 · Cited by 232
Zhou, P.-P., Yuan, M., Song, G., Beutler, N., Shaabani, N., Huang, D., He, W., Zhu, X., Callaghan, S., Yong, P., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9215 · Cited by 196
Greenland, J. R., Michelow, M. D., Wang, L., & London, M. J. (2020) · Anesthesiology · doi:10.1097/aln.0000000000003303 · Cited by 212
Acute kidney injury in SARS-CoV-2 infected patients
Fanelli, V., Fiorentino, M., Cantaluppi, V., Gesualdo, L., Stallone, G., Ronco, C., & Castellano, G. (2020) · Critical Care · doi:10.1186/s13054-020-02872-z · Cited by 203
Kremsner, P., Mann, P., Bosch, J., Fendel, R., Gabor, J. J., Kreidenweiss, A., Kroidl, A., Leroux-Roels, I., Leroux-Roels, G., Schindler, C., et al. (2020) · doi:10.1101/2020.11.09.20228551 · Cited by 199
Being a front-line dentist during the Covid-19 pandemic: a literature review
Fallahi, H. R., Keyhan, S. O., Zandian, D., Kim, S., & Cheshmi, B. (2020) · Maxillofacial Plastic and Reconstructive Surgery · doi:10.1186/s40902-020-00256-5 · Cited by 201
Diagnosis of COVID-19 for controlling the pandemic: A review of the state-of-the-art
Taleghani, N., & Taghipour, F. (2020) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2020.112830 · Cited by 212
MacLean, O. A., Lytras, S., Weaver, S., Singer, J. B., Boni, M. F., Lemey, P., Pond, S. L. K., & Robertson, D. L. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001115 · Cited by 227
Thépaut, M., Luczkowiak, J., Vivès, C., Labiod, N., Bally, I., Lasala, F., Grimoire, Y., Fenel, D., Sattin, S., Thielens, N. M., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009576 · Cited by 222
Type I Interferon (IFN)-Regulated Activation of Canonical and Non-Canonical Signaling Pathways
Mazewski, C., Perez, R. E., Fish, E. N., & Platanias, L. C. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.606456 · Cited by 209
Comparison of transgenic and adenovirus hACE2 mouse models for SARS-CoV-2 infection
Rathnasinghe, R., Strohmeier, S., Amanat, F., Gillespie, V., Krammer, F., García‐Sastre, A., Coughlan, L., Schotsaert, M., & Uccellini, M. B. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1838955 · Cited by 198
Hatmal, M. M., Alshaer, W., Al-Hatamleh, M. A. I., Hatmal, M., Smadi, O., Taha, M. O., Oweida, A., Boer, J. C., Mohamud, R., & Plebanski, M. (2020) · Cells · doi:10.3390/cells9122638 · Cited by 205
Bchetnia, M., Girard, C., Duchaine, C., & Laprise, C. (2020) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2020.07.011 · Cited by 205
SARS-CoV-2 Infects Human Engineered Heart Tissues and Models COVID-19 Myocarditis
Bailey, A. L., Dmytrenko, O., Greenberg, L., Bredemeyer, A. L., Ma, P., Liu, J., Penna, V., Winkler, E. S., Sviben, S., Brooks, E., et al. (2021) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2021.01.002 · Cited by 193
Dhama, K., Patel, S. K., Pathak, M., Yatoo, M. I., Tiwari, R., Malik, Y. S., Singh, R. P., Sah, R., Rabaan, A. A., Bonilla‐Aldana, D. K., et al. (2020) · Travel Medicine and Infectious Disease · doi:10.1016/j.tmaid.2020.101755 · Cited by 196
Case, J. B., Rothlauf, P. W., Chen, R. E., Kafai, N. M., Fox, J. M., Smith, B. K., Shrihari, S., McCune, B. T., Harvey, I. B., Keeler, S. P., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.07.018 · Cited by 185
Amin, S. A., Banerjee, S., Ghosh, K., Gayen, S., & Jha, T. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115860 · Cited by 197
Viral Respiratory Pathogens and Lung Injury
Clementi, N., Ghosh, S., Santis, M. D., Castelli, M., Criscuolo, E., Zanoni, I., Clementi, M., & Mancini, N. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00103-20 · Cited by 202
Naringenin: A flavanone with anti-inflammatory and anti-infective properties
Ji, C., Wen, H., Zhou, H., Zhang, D., Lan, D., Liu, S., Li, C., Dai, X., Song, T., Wang, X., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114990 · Cited by 197
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Lazarević, I., Pravica, V., Miljanovic, D., & Cupic, M. D. (2021) · Viruses · doi:10.3390/v13071192 · Cited by 193
Bohn, M. K., Lippi, G., Horvath, A. R., Sethi, S. K., Koch, D. D., Ferrari, M., Wang, C.-B., Mancini, N., Steele, S., & Adeli, K. (2020) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2020-0722 · Cited by 190
Furin: A Potential Therapeutic Target for COVID-19
Wu, C., Zheng, M., Yang, Y., Gu, X., Yang, K., Li, M., Liu, Y., Zhang, Q., Zhang, P., Wang, Y., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101642 · Cited by 188
Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.015 · Cited by 185
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
Xu, Y., Baylink, D. J., Chen, C.-S., Reeves, M. E., Xiao, J., Lacy, C., Lau, E., & Cao, H. L. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02488-5 · Cited by 191
Sardar, R., Satish, D., Birla, S., & Gupta, D. K. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04658 · Cited by 182
COVID-19 transmission risk and protective protocols in dentistry: a systematic review
Banakar, M., Lankarani, K. B., Jafarpour, D., Moayedi, S., Banakar, M. H., & MohammadSadeghi, A. (2020) · BMC Oral Health · doi:10.1186/s12903-020-01270-9 · Cited by 184
Wang, B., Zhang, L., Wang, Y., Dai, T., Qin, Z., Zhou, F., & Zhang, L. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00986-0 · Cited by 187
Magrone, T., Magrone, M., & Jirillo, E. (2020) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530320666200427112902 · Cited by 186
An In Vitro Microneutralization Assay for SARS‐CoV‐2 Serology and Drug Screening
Amanat, F., White, K. M., Miorin, L., Strohmeier, S., McMahon, M., Meade, P. S., Liu, W., Albrecht, R. A., Simon, V. R., Martínez‐Sobrido, L., et al. (2020) · Current Protocols in Microbiology · doi:10.1002/cpmc.108 · Cited by 171
Davidson, A. M., Wysocki, J. A., & BATLLE, D. C. (2020) · Hypertension · doi:10.1161/hypertensionaha.120.15256 · Cited by 183
Tsai, Y., Lee, C.-L., Yen, H., Chang, Y.-S., Lin, Y.-P., Huang, S., & Lin, C. (2020) · Biomolecules · doi:10.3390/biom10030366 · Cited by 179
Kuzmina, A., Khalaila, Y., Voloshin, O., Keren‐Naus, A., Cohen, L. B., Raviv, Y., Shemer‐Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 177
Immunology of SARS-CoV-2 infection in children
Chou, J. S., Thomas, P. G., & Randolph, A. G. (2022) · Nature Immunology · doi:10.1038/s41590-021-01123-9 · Cited by 176
Autoantibody-negative insulin-dependent diabetes mellitus after SARS-CoV-2 infection: a case report
Hollstein, T., Schulte, D. M., Schulz, J. C., Glück, A., Ziegler, A. G., Bonifacio, E. E., Wendorff, M., Franke, A., Schreiber, S., Bornstein, S. R., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00281-8 · Cited by 181
Prolonged evolution of the human B cell response to SARS-CoV-2 infection
Sakharkar, M., Rappazzo, C. G., Wieland-Alter, W. F., Hsieh, C.-L., Wrapp, D., Esterman, E. S., Kaku, C. I., Wec, A. Z., Geoghegan, J. C., McLellan, J. S., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abg6916 · Cited by 174
Aguiar, J. A., Tremblay, B. J.-M., Mansfield, M. J., Woody, O. Z., Lobb, B., Banerjee, A., Chandiramohan, A., Tiessen, N., Cao, Q., Dvorkin‐Gheva, A., et al. (2020) · European Respiratory Journal · doi:10.1183/13993003.01123-2020 · Cited by 180
Animal and translational models of SARS-CoV-2 infection and COVID-19
Johansen, M. D., Irving, A. T., Montagutelli, X., Tate, M. D., Rudloff, I., Nold, M. F., Hansbro, N. G., Kim, R., Donovan, C., Liu, G., et al. (2020) · Mucosal Immunology · doi:10.1038/s41385-020-00340-z · Cited by 173
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Stadlbauer, D., Tan, J., Jiang, K., Hernandez, M. M., Fabre, S., Amanat, F., Teo, C., Arunkumar, G. A., McMahon, M., Capuano, C., et al. (2020) · Nature · doi:10.1038/s41586-020-2912-6 · Cited by 168
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Glebov, O. O. (2020) · FEBS Journal · doi:10.1111/febs.15369 · Cited by 172
McCallum, M., Walls, A. C., Bowen, J. E., Corti, D., & Veesler, D. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0483-8 · Cited by 166
Broad and Differential Animal Angiotensin-Converting Enzyme 2 Receptor Usage by SARS-CoV-2
Zhao, X., Chen, D., Szabla, R., Zheng, M., Li, G., Du, P., Zheng, S., Li, X., Song, C., Li, R., et al. (2020) · Journal of Virology · doi:10.1128/jvi.00940-20 · Cited by 165
Busnadiego, I., Fernbach, S., Pohl, M. O., Karakus, U., Huber, M., Trkola, A., Stertz, S., & Hale, B. G. (2020) · mBio · doi:10.1128/mbio.01928-20 · Cited by 181
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Edara, V. V., Stuart, A. B., Feng, J., Suthar, M. S., McGuire, A. T., Stamatatos, L., & Pancera, M. (2020) · Nature Communications · doi:10.1038/s41467-020-19231-9 · Cited by 162
Mouffouk, C., Mouffouk, S., Mouffouk, S., Hambaba, L., & Haba, H. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173759 · Cited by 172
Zhai, X., Sun, J., Yan, Z., Zhang, J., Zhao, J., Zhao, Z., Gao, Q., He, W.-T., Veit, M., & Su, S. (2020) · Journal of Virology · doi:10.1128/jvi.00831-20 · Cited by 177
Ou, J., Zhou, Z., Dai, R., Zhang, J., Zhao, S., Wu, X., Lan, W., Ren, Y., Cui, L., Lan, Q., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00617-21 · Cited by 169
Scheaffer, S. M., Lee, D., Whitener, B., Ying, B., Wu, K., Liang, C.-Y., Jani, H., Martin, P., Amato, N. J., Avena, L. E., et al. (2023) · Nature Medicine · doi:10.1038/s41591-022-02092-8 · Cited by 169
Shah, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01021 · Cited by 169
Kang, S., Peng, W., Zhu, Y., Lu, S. Y., Zhou, M., Lin, W., Wu, W., Huang, S., Jiang, L., Luo, X., et al. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105950 · Cited by 166
A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction
Ejemel, M., Li, Q., Hou, S., Schiller, Z. A., Tree, J. A., Wallace, A., Amcheslavsky, A., Yılmaz, N. K., Buttigieg, K. R., Elmore, M. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18058-8 · Cited by 185
Huo, Z., Kim, Y., Suh, I., Lee, D.-M., Lee, J. H., Du, Y., Wang, S., Yoon, H., & Kim, S. (2021) · Nature Communications · doi:10.1038/s41467-021-24028-5 · Cited by 167
Khan, M. T., Ali, A., Wang, Q., Irfan, M., Khan, A., Zeb, M. T., Zhang, Y.-J., Chinnasamy, S., & Wei, D. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1769733 · Cited by 168
Omicron spike function and neutralizing activity elicited by a comprehensive panel of vaccines
Bowen, J. E., Addetia, A., Dang, H. V., Stewart, C., Brown, J. T., Sharkey, W. K., Sprouse, K. R., Walls, A. C., Mazzitelli, I. G., Logue, J. K., et al. (2022) · Science · doi:10.1126/science.abq0203 · Cited by 160
Rauch, S., Roth, N., Schwendt, K., Fotin-Mleczek, M., Mueller, S. O., & Petsch, B. (2021) · npj Vaccines · doi:10.1038/s41541-021-00311-w · Cited by 165
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Katulanda, P., Dissanayake, H. A., Ranathunga, I., Ratnasamy, V., Wijewickrama, P. S. A., Yogendranathan, N., Gamage, K. K. K., de Silva, N. L., Sumanatilleke, M., Somasundaram, N. P., et al. (2020) · Diabetologia · doi:10.1007/s00125-020-05164-x · Cited by 186
Xiong, H., Wu, Y., Cao, J., Yang, R., Liu, Y., Ma, J., Qiao, X., Yao, X., Zhang, B.-H., Zhang, Y., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1815589 · Cited by 155
Zuo, Y. Y., Uspal, W. E., & Wei, T. (2020) · ACS Nano · doi:10.1021/acsnano.0c08484 · Cited by 164
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Huang, J., Song, W., Huang, H., & Sun, Q. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9041131 · Cited by 165
The mechanism and treatment of gastrointestinal symptoms in patients with COVID-19
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History of the COVID-19 pandemic: Origin, explosion, worldwide spreading
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Santesmasses, D., Castro, J. P., Zenin, A. A., Shindyapina, A. V., Gerashchenko, M. V., Zhang, B., Kerepesi, C., Yim, S. H., Fedichev, P. O., & Gladyshev, V. N. (2020) · Aging Cell · doi:10.1111/acel.13230 · Cited by 172
COVID-19: Progress in diagnostics, therapy and vaccination
Liu, X., Liu, C., Liu, G., Luo, W., & Xia, N. (2020) · Theranostics · doi:10.7150/thno.47987 · Cited by 159
Full-genome sequences of the first two SARS-CoV-2 viruses from India
Yadav, P. D., Potdar, V. A., Choudhary, M. L., Nyayanit, D. A., Agrawal, M., Jadhav, S., Majumdar, T., Shete, A. M., Basu, A., Abraham, P., et al. (2020) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_663_20 · Cited by 155
Kumar, K. J. S., Vani, M. G., Wang, C.-H., Chen, C., Chen, Y.-C., Li-ping, L., Huang, C.-H., Lai, C.-S., & Wang, S. (2020) · Plants · doi:10.3390/plants9060770 · Cited by 158
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Padmanabhan, P., Desikan, R., & Dixit, N. M. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008461 · Cited by 152
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Watanabe, Y., Mendonça, L., Allen, E. R., Howe, A., Lee, M., Allen, J. D., Chawla, H., Pulido, D., Donnellan, F. R., Davies, H. D., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00080 · Cited by 155
An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants
Chan, K. K., Tan, T. J. C., Narayanan, K. K., & Procko, E. (2021) · Science Advances · doi:10.1126/sciadv.abf1738 · Cited by 152
“These viruses fall within a common clade of betacoronaviruses that have been experimentally validated to use human ACE2 as an entry receptor (7).”
BackgroundJawad, B., Adhikari, P., Podgornik, R., & Ching, W. Y. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00560 · Cited by 154
Robles, J. P., Zamora, M., Adán‐Castro, E., Siqueiros‐Márquez, L., de la Escalera, G. M., & Clapp, C. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101695 · Cited by 156
Zhou, P.-P., Song, G., Liu, H., Yuan, M., He, W., Beutler, N., Zhu, X., Tse, L. V., Martinez, D. R., Schäfer, A., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.02.005 · Cited by 154
Potential use of polyphenols in the battle against COVID-19
Paraiso, I. L., Revel, J. S., & Stevens, J. F. (2020) · Current Opinion in Food Science · doi:10.1016/j.cofs.2020.08.004 · Cited by 153
Transmission of SARS-CoV-2 from humans to animals and potential host adaptation
Tan, C. C. S., Lam, S. D., Richard, D., Owen, C. J., Berchtold, D., Orengo, C. A., Nair, M. S., Kuchipudi, S. V., Kapur, V., van Dorp, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30698-6 · Cited by 154
Potential Natural Compounds for Preventing SARS-CoV-2 (2019-nCoV) InfectionPreprint
Chen, H., & Du, Q. (2020) · Preprints.org · doi:10.20944/preprints202001.0358.v3 · Cited by 150
Li, Y., Wang, H., Tang, X., Fang, S., Ma, D., Du, C., Wang, Y., Pan, H., Yao, W., Zhang, R., et al. (2020) · Journal of Virology · doi:10.1128/jvi.01283-20 · Cited by 144
Cholesterol, lipoproteins, and COVID-19: Basic concepts and clinical applications
Kočar, E., Režen, T., & Rozman, D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158849 · Cited by 148
Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology
Ribeiro, D. E., Oliveira-Giacomelli, Á., Glaser, T., Arnaud-Sampaio, V. F., Andrejew, R., Dieckmann, L., Baranova, J., Lameu, C., Ratajczak, M. Z., & Ulrich, H. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00965-3 · Cited by 145
COVID‐19 and comorbidities: A role for dipeptidyl peptidase 4 ( DPP4 ) in disease severity?
Bassendine, M. F., Bridge, S. H., McCaughan, G. W., & Gorrell, M. D. (2020) · Journal of Diabetes · doi:10.1111/1753-0407.13052 · Cited by 149
Virology, pathogenesis, diagnosis and in-line treatment of COVID-19
Samudrala, P. K., Kumar, P., Choudhary, K., Thakur, N., Wadekar, G. S., Dayaramani, R. A., Agrawal, M., & Alexander, A. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173375 · Cited by 158
Prospect of SARS-CoV-2 spike protein: Potential role in vaccine and therapeutic development
Samrat, S. K., Tharappel, A. M., Li, Z., & Li, H. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198141 · Cited by 148
Covid-19: Perspectives on Innate Immune Evasion
Taefehshokr, N., Taefehshokr, S., Hemmat, N., & Heit, B. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.580641 · Cited by 152
Bioinformatic prediction of potential T cell epitopes for SARS-Cov-2
Kiyotani, K., Toyoshima, Y., Nemoto, K., & Nakamura, Y. (2020) · Journal of Human Genetics · doi:10.1038/s10038-020-0771-5 · Cited by 145
Engineering luminescent biosensors for point-of-care SARS-CoV-2 antibody detection
Elledge, S. K., Zhou, X. X., Byrnes, J. R., Martinko, A. J., Lui, I., Pance, K., Lim, S. A., Glasgow, J. E., Glasgow, A. A., Turcios, K., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00878-8 · Cited by 146
Epidemiological analysis of COVID‐19 and practical experience from China
Ye, Q., Wang, B., Mao, J., Fu, J., Shang, S., Shu, Q., & Zhang, T. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25813 · Cited by 143
Detection and Characterization of Bat Sarbecovirus Phylogenetically Related to SARS-CoV-2, Japan
Murakami, S., Kitamura, T., Suzuki, J., Sato, R., Aoi, T., Fujii, M., Matsugo, H., Kamiki, H., Ishida, H., Takenaka‐Uema, A., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2612.203386 · Cited by 138
Correlates of critical illness-related encephalopathy predominate postmortem COVID-19 neuropathology
Deigendesch, N., Sironi, L., Kutza, M., Wischnewski, S., Fuchs, V., Hench, J., Frank, A., Nienhold, R., Mertz, K. D., Cathomas, G., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02213-y · Cited by 142
Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell
Puray‐Chavez, M., LaPak, K. M., Schrank, T. P., Elliott, J. L., Bhatt, D. P., Agajanian, M. J., Jasuja, R., Lawson, D. Q., Davis, K., Rothlauf, P. W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109364 · Cited by 139
Drug repurposing strategies for COVID-19
Senanayake, S. L. (2020) · Future Drug Discovery · doi:10.4155/fdd-2020-0010 · Cited by 141
SARS-CoV-2 productively infects primary human immune system cells in vitro and in COVID-19 patients
Pontelli, M. C., Castro, Í. A., Júnior, R. B. M., Serra, L. L., Veras, F. P., Nascimento, D. C., Silva, C. M. S., Cardoso, R. D. S., Rosales, R., Gomes, R., et al. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac021 · Cited by 141
COVID-19 and the Kidneys: An Update
Benedetti, C., Waldman, M. A., Zaza, G., Riella, L. V., & Cravedi, P. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00423 · Cited by 145
Optimized Pseudotyping Conditions for the SARS-COV-2 Spike Glycoprotein
Johnson, M. C., Lyddon, T. D., Suarez, R., Salcedo, B., LePique, M., Graham, M., Ricana, C. L., Robinson, C. A., & Ritter, D. G. (2020) · Journal of Virology · doi:10.1128/jvi.01062-20 · Cited by 143
Hassan, A. O., Feldmann, F., Zhao, H., Curiel, D. T., Okumura, A., Tang-Huau, T.-L., Case, J. B., Meade-White, K. D., Callison, J. A., Chen, R. E., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100230 · Cited by 137
Fagre, A. C., Lewis, J., Eckley, M., Zhan, S., Rocha, S. M., Sexton, N. R., Burke, B. E., Geiss, B. J., Peersen, O. B., Bass, T. A., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009585 · Cited by 145
Citrus fruits are rich in flavonoids for immunoregulation and potential targeting ACE2
Liu, W., Zheng, W., Cheng, L., Ming, L., Huang, J., Bao, S., Xu, Q., & Ma, Z. (2022) · Natural Products and Bioprospecting · doi:10.1007/s13659-022-00325-4 · Cited by 140
Schuler, B. A., Habermann, A. C., Plosa, E. J., Taylor, C. J., Jetter, C. S., Kapp, M., Benjamin, J. T., Gulleman, P., Nichols, D. S., Braunstein, L. Z., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci140766 · Cited by 136
Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry
Park, Y., Marco, A. D., Starr, T. N., Liu, Z., Pinto, D., Walls, A. C., Zatta, F., Zepeda, S. K., Bowen, J. E., Sprouse, K. R., et al. (2022) · Science · doi:10.1126/science.abm8143 · Cited by 135
Pharmacological perspective: glycyrrhizin may be an efficacious therapeutic agent for COVID-19
Luo, P., Liu, D., & Li, J. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105995 · Cited by 142
Metadata
- Authors
- Letko, M., Marzi, A., & Munster, V.
- Affiliations
- National Institutes of Health (US)
- National Institute of Allergy and Infectious Diseases (US)
- Corresponding author
- Letko, Michael
- Munster, Vincent
- Venue
- Nature Microbiology
- Published
- 2020-02-24
- Volume
- 5
- Issue
- 4
- Pages
- 562-569
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC7095430
- OpenAlex
- W3008394341
- Cited by
- 3,109
- References
- 38
- Citations by year
- 2026: 47 · 2025: 122 · 2024: 198 · 2023: 287 · 2022: 571 · 2021: 874 · 2020: 1002
- FWCI
- 89.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Microbiology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Chinese Center for Disease Control and Prevention
- Chinese Academy of Medical Sciences
- Peking Union Medical College
- National Institute of Allergy and Infectious Diseases
- Topics
- 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
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Zoonotic diseases and public health
- Keywords
- SARS-CoV-2, SARS-CoV, cell entry, ACE2 receptor, zoonotic transmission, viral recombination, cross-species infection
- MeSH terms
- Protein Domains, Betacoronavirus, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Cell Line, Humans, Peptidyl-Dipeptidase A, Mutation, Pneumonia, Viral, Receptors, Virus, Recombinant Fusion Proteins, Trypsin, Coronavirus Infections, Dipeptidyl Peptidase 4, CD13 Antigens, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Pandemics, Spike Glycoprotein, Coronavirus
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